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2,3,5,6-tetramethyl-p-phenylendiamine + O2 + H+
? + H2O
-
-
-
-
?
2,3,5,6-tetramethyl-p-phenylenediamine + O2
? + H2O
3,3'-diaminobenzidene-tetrahydrochloride + O2 + H+
? + H2O
4 ferrocytochrome c + O2 + 4 H+
4 ferricytochrome c + 2 H2O
4 ferrocytochrome c + O2 + 4 H+/in
4 ferricytochrome c + 2 H2O
amidopyrine + H2O2
?
-
-
-
-
?
ascorbate + O2
?
-
-
-
-
?
ascorbate + O2
? + H2O
-
reaction of enzyme in detergent solution and reconstituted in phospholipid vesicles
-
-
?
benzidine + H2O2
?
-
-
-
-
?
diaminobenzidine + H2O2
?
-
-
-
-
?
diaminodurene + O2 + H+
?
-
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
ferrocytochrome c + O2
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
ferrocytochrome c(H) + O2
ferricytochrome c(H) + H2O
-
-
-
-
?
ferrocytochrome c-550 + O2
ferricytochrome c-550 + H2O
-
-
-
-
?
ferrocytochrome c549 + O2 + H+
ferricytochrome c549 + H2O
-
-
-
-
r
ferrocytochrome c550 + O2 + H+
ferricytochrome c550 + H2O
ferrocytochrome c551 + O2 + H+
ferricytochrome c551 + H2O
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
ferrocytochrome c553 + O2 + H+
ferricytochrome c553 + H2O
-
-
-
-
r
melatonin + H2O2
?
-
-
-
-
?
N,N,N',N'-tetramethyl-4-phenylendiamine + O2 + H+
?
N,N,N',N'-tetramethyl-p-phenylenediamine + O2
?
-
-
-
-
?
O2 + 4 cyt c(Fe2+) + 8 H+/in
2 H2O + 4 cyt c(Fe3+) + 4 H+/out
oxidized horse heart cytochrome c + H2O
reduced horse heart cytochrome c + O2 + H+
-
-
-
-
?
p-phenylenediamine + H2O2
?
-
-
-
-
?
peroxynitrite
NO + O22-
-
enzyme must be fully reduced, proposed reaction
-
?
phenazine methosulfate + O2 + H+
?
-
-
-
-
?
reduced ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + H2O
reduced ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine + H2O
-
-
-
-
r
reduced ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + H2O
reduced Aspergillus oryzae cytochrome c + O2
oxidized Aspergillus oryzae cytochrome c + H2O
-
relative activity 2.2%
-
-
?
reduced Bacillus subtilis cytochrome c + O2
oxidized Bacillus subtilis cytochrome c + H2O
-
relative activity 27%
-
-
?
reduced Bos taurus cytochrome c + O2
oxidized Bos taurus cytochrome c + H2O
reduced Bos taurus cytochrome c + O2 + H+
oxidized Bos taurus cytochrome c + H2O
-
-
-
-
?
reduced Bufo vulgaris cytochrome c + O2
oxidized Bufo vulgaris cytochrome c + H2O
-
relative activity 0.73%
-
-
?
reduced Candida krusei cytochrome c + O2
oxidized Candida krusei cytochrome c + H2O
-
relative activity 5.0%
-
-
?
reduced Columba livia cytochrome c + O2
oxidized Columba livia cytochrome c + H2O
-
relative activity 0.44%
-
-
?
reduced cytochrome aa3 + O2 + H+
oxidized cytochrome aa3 + H2O
-
formation of a tryptophan-radical intermediate (tryptophan neutral radical of the strictly conserved Trp-272). The formation of the Trp-272 constitutes the major rate-determining step of the catalytic cycle
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
reduced cytochrome c551 + O2 + H+
oxidized cytochrome c551 + H2O
reduced Homo sapiens cytochrome c + O2
oxidized Homo sapiens cytochrome c + H2O
-
relative activity 0.44%
-
-
?
reduced horse cytochrome c + O2
oxidized horse cytochrome c + H2O
reduced horse cytochrome c + O2 + H+
oxidized horse cytochrome c + H2O
reduced horse heart cytochrome c + O2 + H+
oxidized horse heart cytochrome c + H2O
reduced Kloeckera sp. cytochrome c + O2
oxidized Kloeckera sp. cytochrome c + H2O
-
relative activity 5.4%
-
-
?
reduced Loligo pealeii cytochrome c + O2
oxidized Loligo pealeii cytochrome c + H2O
-
relative activity 1.2%
-
-
?
reduced Musca domestica cytochrome c + O2
oxidized Musca domestica cytochrome c + H2O
-
relative activity 2.6%
-
-
?
reduced N,N,N',N'-tetramethyl-4-phenylenediamine + O2 + H2
oxidized N,N,N',N'-tetramethyl-4-phenylenediamine + H2O
reduced N,N,N',N'-tetramethyl-p-phenylene diamine + O2
oxidized N,N,N',N'-tetramethyl-p-phenylene diamine + H2O
reduced oyster cytochrome c + O2
oxidized oyster cytochrome c + H2O
-
relative activity 0.54%
-
-
?
reduced Physarum polycephalum cytochrome c + O2
oxidized Physarum polycephalum cytochrome c + H2O
-
relative activity 0.9%
-
-
?
reduced Porphyra tenera cytochrome c + O2
oxidized Porphyra tenera cytochrome c + H2O
-
relative activity 15%
-
-
?
reduced prawn cytochrome c + O2
oxidized prawn cytochrome c + H2O
-
relative activity 0.95%
-
-
?
reduced Pseudomonas aeruginosa cytochrome c + O2
oxidized Pseudomonas aeruginosa cytochrome c + H2O
-
relativ activity 100%
-
-
?
reduced Pseudomonas saccharophila cytochrome c + O2
oxidized Pseudomonas saccharophila cytochrome c + H2O
-
relative activity 82%
-
-
?
reduced Rhodospirillum rubrum cytochrome c + O2
oxidized Rhodospirillum rubrum cytochrome c + H2O
-
relative activity 1.7%
-
-
?
reduced Saccharomyces cerevisiae cytochrome c + O2
oxidized Saccharomyces cerevisiae cytochrome c + H2O
-
relative activity 4.9%
-
-
?
reduced salmon cytochrome c + O2
oxidized salmon cytochrome c + H2O
-
relative activity 7.1%
-
-
?
reduced Scombridae gen. sp. cytochrome c + O2
oxidized Scombridae gen. sp. cytochrome c + H2O
-
relative activity 8.7%
-
-
?
reduced shark cytochrome c + O2
oxidized shark cytochrome c + H2O
-
relative activity 1.5%
-
-
?
reduced Styela plicata cytochrome c + O2
oxidized Styela plicata cytochrome c + H2O
-
relative activity 2.2%
-
-
?
reduced Triticum aestivum cytochrome c + O2
oxidized Triticum aestivum cytochrome c + H2O
-
relative activity 1.5%
-
-
?
reduced yeast cytochrome c + O2
oxidized yeast cytochrome c + H2O
tetramethyl-phenylenediamine + O2 + H+
? + H2O
-
-
-
-
?
tetramethylbenzidine + H2O2
?
-
-
-
-
?
additional information
?
-
2,3,5,6-tetramethyl-p-phenylenediamine + O2
? + H2O
-
-
-
-
?
2,3,5,6-tetramethyl-p-phenylenediamine + O2
? + H2O
-
-
-
-
?
3,3'-diaminobenzidene-tetrahydrochloride + O2 + H+
? + H2O
-
-
-
?
3,3'-diaminobenzidene-tetrahydrochloride + O2 + H+
? + H2O
-
-
-
?
3,3'-diaminobenzidene-tetrahydrochloride + O2 + H+
? + H2O
-
-
-
-
?
4 ferrocytochrome c + O2 + 4 H+
4 ferricytochrome c + 2 H2O
-
-
-
?
4 ferrocytochrome c + O2 + 4 H+
4 ferricytochrome c + 2 H2O
-
-
-
?
4 ferrocytochrome c + O2 + 4 H+/in
4 ferricytochrome c + 2 H2O
-
-
-
-
?
4 ferrocytochrome c + O2 + 4 H+/in
4 ferricytochrome c + 2 H2O
-
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
-
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
-
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
additional electron donor: rusticyanin, i.e. a copper protein from Thiobacillus ferrooxidans
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
ferrocytochrome c552
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
flavin semiquinone electron donors lumiflavin, riboflavin or FMN can be used, kinetic analysis
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Saccharomyces cerevisiae cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: 2,6-dichlorophenolindophenol
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: phenazine methosulfate
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Candida krusei ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/hexaamine ruthenium
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
proton translocation across eukaryotic mitochondrial and prokyryotic cytoplasmic membrane, overview proposed mechanims
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
reaction intermediates
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
terminal enzyme of the electron transport chain. The glucagon receptor/G-protein/c-AMP pathway regulates enzyme activity
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
no proton translocation
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Crithidia fasciculata cytochrome c
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Saccharomyces cerevisiae cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
flavin semiquinone electron donors lumiflavin, riboflavin or FMN can be used, kinetic analysis
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
cytochrome c550 and cytochrome c549
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Candida krusei ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
proton translocation across eukaryotic mitochondrial and prokyryotic cytoplasmic membrane, overview proposed mechanims
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
overview additional activities i.e. catalase activity, peroxidase activity, superoxide dismutase activity, carbomonoxygenase activity
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Saccharomyces cerevisiae cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: phenazine methosulfate
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Saccharomyces cerevisiae cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
flavin semiquinone electron donors lumiflavin, riboflavin or FMN can be used, kinetic analysis
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Magnetospirillum magnetotacticum cytochrome c550
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/diaminodurene
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: phenazine methosulfate
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
coordinated down regulation of mitochondrial genome-coded CytOX I and CytOX II and nuclear genome-coded CytOX IV and Vb mRNAs during hypoxia
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Nitrobacter agilis ferrocytochrome c552
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Saccharomyces oviformis cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
cow cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
ferrocytochrome c550
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
tuna cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Candida krusei ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Nitrosomonas europaea cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Candida krusei ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Nitrosomonas europaea cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Candida krusei ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Candida krusei ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
coordinated down regulation of mitochondrial genome-coded CytOX I and CytOX II and nuclear genome-coded CytOX IV and Vb mRNAs during hypoxia
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Saccharomyces cerevisiae cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
cow cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
tuna cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
cytochrome c6 is at least one of the endogenous electron donors. In the thylakoid lumen cytochrome c6 can deliver electrons to cytochrome c oxidase
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Candida krusei ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: phenazine methosulfate
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184 -
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
Saccharomyces cerevisiae cytochrome c
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
horse cytochrome c
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
Thermus thermophilus cytochrome c
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
Candida krusei cytochrome c
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c550 + O2 + H+
ferricytochrome c550 + H2O
-
-
-
-
r
ferrocytochrome c550 + O2 + H+
ferricytochrome c550 + H2O
-
-
-
-
r
ferrocytochrome c550 + O2 + H+
ferricytochrome c550 + H2O
-
-
-
-
r
ferrocytochrome c551 + O2 + H+
ferricytochrome c551 + H2O
-
-
-
-
r
ferrocytochrome c551 + O2 + H+
ferricytochrome c551 + H2O
-
-
-
-
r
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
-
-
-
-
r
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
-
-
-
-
r
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
-
-
-
-
r
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
-
-
-
-
r
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
-
-
-
-
r
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
-
-
-
-
r
N,N,N',N'-tetramethyl-4-phenylendiamine + O2 + H+
?
-
-
-
-
?
N,N,N',N'-tetramethyl-4-phenylendiamine + O2 + H+
?
-
-
-
-
?
N,N,N',N'-tetramethyl-4-phenylendiamine + O2 + H+
?
-
-
-
-
?
N,N,N',N'-tetramethyl-4-phenylendiamine + O2 + H+
?
-
-
-
-
?
o-dianisidine + H2O2
?
-
-
-
-
?
o-dianisidine + H2O2
?
-
-
-
-
?
o-dianisidine + H2O2
?
-
-
-
-
?
O2 + 4 cyt c(Fe2+) + 8 H+/in
2 H2O + 4 cyt c(Fe3+) + 4 H+/out
-
-
-
?
O2 + 4 cyt c(Fe2+) + 8 H+/in
2 H2O + 4 cyt c(Fe3+) + 4 H+/out
-
-
-
?
reduced ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + H2O
-
-
-
-
r
reduced ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + H2O
-
-
-
-
r
reduced ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + H2O
-
-
-
-
?
reduced ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + H2O
-
-
-
-
?
reduced Bos taurus cytochrome c + O2
oxidized Bos taurus cytochrome c + H2O
-
-
-
-
?
reduced Bos taurus cytochrome c + O2
oxidized Bos taurus cytochrome c + H2O
-
-
-
-
?
reduced Bos taurus cytochrome c + O2
oxidized Bos taurus cytochrome c + H2O
-
relative activity 0.53%
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
-
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
oxidation of cytochrome c by cytochrome oxidase stimulates caspase activation
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
-
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
-
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
-
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
-
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
electron exchange of cytochrome c with the electrode with CcO (with a his-tag at the C-terminus of subunit I) immobilized in a protein-tethered bilayer lipid membrane is shown to be mediated by the enzyme if oxygen is present in the bulk solution. The increasing current density in the anodic and cathodic direction in the presence of oxygen may be due to intermediate redox states of the CcO. Hopping mechanism of electron transfer through the enzyme between cytochrome c and the electrode
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
-
-
-
?
reduced cytochrome c551 + O2 + H+
oxidized cytochrome c551 + H2O
-
-
-
-
?
reduced cytochrome c551 + O2 + H+
oxidized cytochrome c551 + H2O
-
-
-
-
?
reduced horse cytochrome c + O2
oxidized horse cytochrome c + H2O
-
-
-
-
?
reduced horse cytochrome c + O2
oxidized horse cytochrome c + H2O
-
-
-
-
?
reduced horse cytochrome c + O2 + H+
oxidized horse cytochrome c + H2O
-
-
-
-
?
reduced horse cytochrome c + O2 + H+
oxidized horse cytochrome c + H2O
-
-
-
-
?
reduced horse heart cytochrome c + O2 + H+
oxidized horse heart cytochrome c + H2O
-
-
-
-
?
reduced horse heart cytochrome c + O2 + H+
oxidized horse heart cytochrome c + H2O
-
-
-
-
?
reduced N,N,N',N'-tetramethyl-4-phenylenediamine + O2 + H2
oxidized N,N,N',N'-tetramethyl-4-phenylenediamine + H2O
-
-
-
-
?
reduced N,N,N',N'-tetramethyl-4-phenylenediamine + O2 + H2
oxidized N,N,N',N'-tetramethyl-4-phenylenediamine + H2O
-
-
-
-
?
reduced N,N,N',N'-tetramethyl-p-phenylene diamine + O2
oxidized N,N,N',N'-tetramethyl-p-phenylene diamine + H2O
-
-
-
-
?
reduced N,N,N',N'-tetramethyl-p-phenylene diamine + O2
oxidized N,N,N',N'-tetramethyl-p-phenylene diamine + H2O
-
-
-
-
?
reduced yeast cytochrome c + O2
oxidized yeast cytochrome c + H2O
-
-
-
-
?
reduced yeast cytochrome c + O2
oxidized yeast cytochrome c + H2O
-
-
-
-
?
additional information
?
-
-
accessibility and electrostatic charge of enzyme do not differ in a significant way among human, Arabidopsis thaliana and horse
-
-
?
additional information
?
-
-
numerous organic aromatic compounds, which are not oxidized by cytochrome oxidase via the oxidase mechanism (i.e. using molecular oxygen as the terminal acceptor), can undergo a low rate oxidation by cytochrome oxidase via the peroxidase mechanism. Paracetamol and isonicotinic acid hydrazide are completely resistant to peroxidation by cytochrome oxidase
-
-
?
additional information
?
-
-
cytochrome c oxidase is an efficient energy transducer that reduces oxygen to water and converts the released chemical energy into an electrochemical membrane potential. As a true proton pump, the enzyme translocates protons across the membrane against this potential
-
-
?
additional information
?
-
-
the predominant entry point for protons going into the K-channel of cytochrome oxidase is the surface-exposed glutamic acid E101 in subunit II
-
-
?
additional information
?
-
-
accessibility and electrostatic charge of enzyme do not differ in a significant way among human, Arabidopsis thaliana and horse
-
-
?
additional information
?
-
-
accessibility and electrostatic charge of enzyme do not differ in a significant way among human, Arabidopsis thaliana and horse
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
additional information
?
-
-
the enzyme also shows catalase activity
-
-
?
additional information
?
-
For all mutant strains, the NADH oxidation activity of membranes obtained from aerobic exponentially growing cultures is some higher than that of the wild-type strain (in the range of 1035% higher)
-
-
?
additional information
?
-
-
For all mutant strains, the NADH oxidation activity of membranes obtained from aerobic exponentially growing cultures is some higher than that of the wild-type strain (in the range of 1035% higher)
-
-
?
additional information
?
-
inactivation of the Cbb3-1 terminal oxidase in a strain containing a wild-type ANR gene lead to a 46% decrease in cytochrome b and to a 57% decrease in cytochrome c
-
-
?
additional information
?
-
-
inactivation of the Cbb3-1 terminal oxidase in a strain containing a wild-type ANR gene lead to a 46% decrease in cytochrome b and to a 57% decrease in cytochrome c
-
-
?
additional information
?
-
For all mutant strains, the NADH oxidation activity of membranes obtained from aerobic exponentially growing cultures is some higher than that of the wild-type strain (in the range of 1035% higher)
-
-
?
additional information
?
-
inactivation of the Cbb3-1 terminal oxidase in a strain containing a wild-type ANR gene lead to a 46% decrease in cytochrome b and to a 57% decrease in cytochrome c
-
-
?
additional information
?
-
-
thyroid hormone T3 regulates the expression of COX subunits by both transcriptional and posttranslational mechanism
-
-
?
additional information
?
-
-
cytochrome c purified from mammalian brain is phosphorylated on S47, phosphorylation is lost during ischemia. Both S47-phosphorylated and phosphomimetic cytochrome c show a lower oxygen consumption rate in reaction with isolated Cytc oxidase
-
-
?
additional information
?
-
-
the intermolecular electron transfer kinetics between CytcM and the soluble CuA domain, i.e. the donor binding and electron entry site, of subunit II of cytochrome c oxidase is investigated
-
-
?
additional information
?
-
-
oxygenation of the tetradentate model both in MeCN and in other solvents produces a low-temperature-stable dioxygen-bridged peroxide with an O-O stretching vibration at 799 cm-1. Oxygenation of the tridentate model in EtCN solution generates a heme superoxide species with the copper moiety oxidized to copper(II). Coexistence of a heme superoxide and a bridged peroxide species in equivalent amounts when the oxygenation reaction is carried out in CH2Cl2/7% EtCN
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
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4-hydroxynonenal
-
time- and concentration-dependent inhibition of cytochrome c oxidase activity. Superoxide dismutase and catalase and the HO radical scavenger mannitol partially prevent inhibition of cytochrome c oxidase activity
aluminium phosphite
-
decrease in catalytic efficiency of active enzyme molecules on treatment with aluminium phosphide
amyloid beta
-
native, up to 65% inhibition. Amyloid beta mutation Y10A does not affect maximal inhibition, but the altered peptide needs a longer period for ageing. Substitution M35V or oxidizing the sulfur of M35 to a sulfoxide completely abrogates the peptides inhibitory potential. Inhibition depends completely on presence of divalent Cu2+ and may involve the formation of a redox active amyloid-beta-methionine radical
-
amyloid beta1-42
-
synthetic peptide, dimeric amyloid beta specifically inhibits the cytochrome-c oxidase dependent on presence of Cu2+ and specific ageing of the amyloid beta1-42 solution
-
bilirubin
-
0.05 mM serum unconjugated bilirubin rapidly and selectively inhibits cytochrome c oxidase activity. Pre-treatment of neurons with 0.05 mM glycoursodeoxycholic acid prior to exposure to serum unconjugated bilirubin prevents inhibition of cytrochrome c oxidase activity
Cl-
-
80 mM, complete inhibition
Cu2+
-
inhibition of enzyme by amyloid beta depends completely on presence of divalent Cu2+, but not Cu+
diethylenetriamine-NONOate
-
-
dodecyl beta-D-maltopyranoside
-
ethylene glycol
-
inhibits by reducing electron flow between cytochrome a and cytochrome a3
Hg2+
-
cytochrome c oxidase activities of strains AP19-3 and ATCC 23270 are completely inhibited by 0.001 mM and 0.005 mM. Strain MON-1 is inhibited 33% by 0.005 mM, and 70% by 0.010 mM
high ionic strength
-
above 200 mM KCl
-
HIV-1 neurotoxin trans activator of transcription protein
-
inhibits the electron transport chain in a concentration-dependent manner. A concentration of 5 ng/ml, 50 ng/ml, and 10 microg/ml inhibit activity to 84, 47, and 35% of control, respectively
-
Lithium diiodosalicylate
-
-
miltefosine
-
inhibits in a dose-dependent manner. CcO appears to be an important target, as inhibition by this drug runs parallel to the alteration of processes such as O2 consumption and mitochondrial membrane potential, as well as the drop in ATP levels
N,N-Dimethyllauryl amine oxide
-
-
NaCN
-
1 mM completely inhibits mercury volatilization activities with reduced cytochrome c and 2,3,5,6-tetramethyl-p-phenylendiamine in strain MON-1
NH2OH
-
3 mM, 80% inhibition
NO2-
-
competitive inhibitor
nonionic detergents
-
-
-
peroxynitrite
-
0.1 mM, complete inhibition
poly-L-lysine
-
complete inhibition of horse and Candida krusei cytochrome c oxidation with 0.0001 mM and 0.002 mM poly-L-lysine, respectively
siRNA
-
small interfering RNA against Vb selectively lowers COX Vb expression in HeLa-80 cells, increases mitochondrial reactive oxygen species generation, decreases COX activity 60-80%, and diminishes viability under 80% (but not 20%) O2
-
theophylline
-
at therapeutic concentrations used for asthma relief, theophylline causes inhibition of the lung enzyme and decreases cellular ATP levels, suggesting a mechanism for its clinical action
trans-[RuCl2(3,4-pyridinedicarboxylic acid)4]Cl
-
inhibits COX activity in kidney
-
trans-[RuCl2(3-pyridinecarboxylic acid)4]
-
inhibits COX activity in heart and kidney
trans-[RuCl2(4-pyridinecarboxylic acid)4]
-
inhibits COX activity in hippocampus, heart, liver and kidney
Tumor necrosis factor alpha
-
Tween 20
-
0.5%, 40% inhibition
Tween 80
-
0.5% 60% inhibition
ATP
-
the ATP-inhibition of CcO is only effective at very high ATP/ADP ratios (above 50) in the mitochondrial matrix or at low concentrations of ferrocytochrome c
ATP
-
the ATP-inhibition of CcO is only effective at very high ATP/ADP ratios (above 50) in the mitochondrial matrix or at low concentrations of ferrocytochrome c
ATP
-
ATP inhibition occurs under uncoupled conditions (in the presence of carbonly cyanide m-chlorophenyl hydrazine) when the classical respiratory control is absent. High ATP/ADP ratios in the matrix as well as in the cytosolic space are required for full ATP inhibition of the enzyme
azide
-
1 mM, 60% inhibition
azide
-
0.08 mM, 50% inhibition
azide
-
0.1 mM, 50% inhibition
azide
-
heme-binding inhibitor, noncompetitive vs. O2 and cytochrome c
azide
-
0.08 mM, 50% inhibition
azide
-
1 mM, 50% inhibition of horse cytochrome c oxidation, 0.85 mM, 50% inhibition of horse cytochrome c oxidation in the presence of cardiolipin, 6.5 mM, 50% inhibition of Candida krusei cytochrome c oxidation, 1.5 mM, 50% inhibition of Nitrosomonas europaea cytochrome c oxidation
azide
-
uncompetitive inhibitor, inhibits the oxidase activity both in hypoxia and normoxia
azide
-
0.007 mM, 50% inhibition, 1 mM, complete inhibition
azide
-
0.014 mM, 50% inhibition of tuna cytochrome c oxidation
azide
-
0.11 mM, 50% inhibition, 10 mM, complete inhibition
CN-
-
0.1 mM, 96% inhibition
CN-
-
0.001 mM, 50% inhibition
CN-
-
0.02 mM, inhibition of peroxynitrite reduction
CN-
-
0.0013 mM, 50% inhibition
CN-
-
heme-binding inhibitor, noncompetitive vs. O2 and cytochrome c
CN-
-
0.0001 mM, 50% inhibition
CN-
-
0.012 mM, 50% inhibition
CN-
-
0.001 mM, 59% inhibition
CN-
-
0.001 mM, 50% inhibition
CN-
-
0.13 mM, 50% inhibition of horse cytochrome c oxidation, 0.08 mM 50% inhibition of horse and Candida krusei cytochrome c oxidation in the presence of cardiolipin, 0.06 mM, 50% inhibition of Candida krusei cytochrome c oxidation, 0.05 mM, 50% inhibition of Nitrosomonas europaea cytochrome c oxidation
CN-
-
0.003 mM, 50% inhibition
CN-
-
10 mM, complete inhibition
CN-
-
0.0005 mM, 50% inhibition
CN-
-
0.004 mM, 50% inhibition of tuna cytochrome c oxidation
CN-
-
0.0012 mM, complete inhibition
CN-
-
0.0013 mM, 50% inhibition, 1 mM, complete inhibition
CN-
-
0.0012 mM, complete inhibition
CO
-
competitive vs. O2
CO
-
competitive and reversible
CO
-
competitive inhibitor
CO
-
significantly decreases myocardial CcOX activity. CcOX I protein levels significantly decrease following CO exposure while enzyme turnover number and CcOX I mRNA levels remain unchanged. Decreased CcOX activity following CO inhalation is likely due to decreased heme aa3 and CcOX subunit I content
CO
-
inhibits cytochrome c oxidase activity by 50%. Acts via inhibition of cytochrome c oxidase leading to the generation of low levels of reactive oxygen species that in turn mediate subsequent adaptive signaling. CO inhibits cytochrome c oxidase, while maintaining cellular ATP levels and increasing mitochondrial membrane potential
cyanide
-
-
cyanide
-
Pseudomonas fluorescens strain CHA0 can kill Odontotermes obesus by inhibiting cytochrome c oxidase of the termite respiratory chain with the pseudomonad metabolite cyanide after a 2 h incubation period
Dicyclohexylcarbodiimide
-
-
Dicyclohexylcarbodiimide
-
inhibition of redox-linked proton translocation
F-
-
-
KCl
-
20 mM, 50% inhibition
KCl
-
50 mM, 50% inhibition
KCN
-
1 mM results in a sustained 50% loss of activity following 24, 48 and 72 h of culture
KCN
1 mM inhibits all terminal oxidases excepting the CIO quinol oxidase and lead to reduced NADH oxidation between 2.5- and 4fold
KCN
-
1 mM completely inhibits
N3-
-
non-competitive inhibitor
NaN3
-
-
NaN3
-
reduces COx activity in homogenates of the cortex and hippocampus by 40% and 37% respectively, 4 weeks after pump implantation
nitric oxide
-
competitive and reversible. Nanomolar levels inhibit the enzyme by competing with oxygen at the enzymes heme-copper active site. This raises the Km for cellular respiration into the physiological range
nitric oxide
-
steady-state and kinetic modeling of inhibition. NO interacts with either ferrous heme iron or oxidized copper, but not both simultaneously. The affinity of NO for the oxygen-binding ferrous heme site is 0.2 nM
nitric oxide
-
partial inhibition of cytochrome-c oxidase by nitric oxide leads to an accumulation of reduced cytochrome c and to an increase in electron flux through the enzyme population not inhibited by nitric oxide
nitric oxide
-
nitric oxide that is not inactivated inhibits the cytochrome c oxidase, reducing the enzyme and lowering O2 consumption
nitric oxide
-
nitric oxide generated from NaNO2 decreases cellular oxygen consumption and inhibits CcOX activity
NO
-
competitive vs. O2
NO
-
competitive inhibitor
NO
-
irreversibly inhibits in a reverse oxygen concentration-dependent manner. COX activity is decreased from 51.3% at 0.2 mM and to 3.8% at 0.025 mM. Inhibition is dramatically protected by a peroxynitrite scavenger, which is formed from the reaction of NO with cytochrome oxidase at low oxygen concentration, and that is involved in irreversible cytochrome oxidase inactivation. Nitroxyl anion scavenger potently protects the irreversible inhibition, whereas a superoxide dismutase does not provide protective effect, suggesting that the peroxynitrite is formed from nitroxyl anion rather than the reaction of NO with superoxide
NO
-
inhibits cytochrome oxidase in competition with oxygen. Hypoxia (2% O2) markedly inhibits cytochrome oxidase activity (relative to normoxia), and N-4S-4-amino-5-2-aminoethylaminopentyl-N'-nitroguanidine reverses this inhibition in the presence of hypoxia, but has no effect in normoxia
NO
-
increased NO production after traumatic brain injury triggers inhibition of CcO. Traumatic brain injury leads to CcO inhibition and dramatically decreased ATP levels in brain cortex. CcO inhibition can be partially restored by application of iNOS antisense oligonucleotides prior to traumatic brain injury, which leads to a normalization of ATP levels similar to the controls
NO
-
simple dynamic steady-state non-equilibrium model. Binding to the oxidase is always proportional to the degree of inhibition of oxygen consumption. Primary effect of NO binding to the oxidised enzyme is to convert NO to nitrite, rather than to inhibit enzyme activity
phosphate
-
-
phosphate
-
more than 15 mM
phosphate
-
more than 70 mM
phosphate
-
more than 10 mM
phosphate
-
not with yeast cytochrome c
phosphate
-
more than 10 mM
potassium cyanide
-
2 mM inhibits electron flow from complex IV to oxygen
potassium cyanide
-
0.25 mM potassium cyanide completely and reversibly inhibits both the electron and proton transport function of COX, the addition of 60 mM pyruvate induces the maximal recovery of both parameters to 60-80% of the original values. Low KCN concentrations of up to 0.005 mM lead to a profound, 30fold decrease of COX affinity for oxygen
potassium cyanide
-
cyanide binds to the binuclear heme center of cytochrome c oxidase, complete inhibition at 0.02 mM, pretreatment with NaNO2 reverses potassium cyanide-mediated inhibition of CcOX activity
Salicyl aldoxime
-
-
Sodium azide
-
the addition of 0.5 mM sodium azide at 0.1 mM O2during the initial purging process results in a maximal reduction in cytochrome c oxidase redox state
Sodium azide
-
5 mM inhibits electron flow from complex IV to oxygen
Sulfide
-
-
Sulfide
-
heme-binding inhibitor, noncompetitive vs. O2 and cytochrome c
Triton X-100
-
-
Triton X-100
-
0.3%, 50% inhibition
Tumor necrosis factor alpha
-
leads to an ca. 60% reduction in CcO activity in hepatocyte homogenates. Shows no direct effect on CcO activity using purified CcO. CcO isolated after tumor necrosis factor alpha treatment shows tyrosine phosphorylation on CcO catalytic subunit I and is ca. 50 and 70% inhibited at high cytochrome c concentrations in the presence of allosteric activator ADP and inhibitor ATP, respectively
-
Tumor necrosis factor alpha
-
leads to reduction in CcO activity in hepatocyte homogenates. Shows no direct effect on CcO activity using isolated mitochondria CcO
-
Zn2+
-
tetrahedral coordination of Zn2+ with two N-histidine imidazoles, one N-histidine imidazol or N-lysine and one O-COOH, possibly located at the entry site ogf the proton conducting D pathway; tetrahedral coordination site(s) for Zn2+ with two N-histidine imidazoles, one N-histidine imidazol or N-lysine and one O-COOH (glutamate or aspartate), possibly located at the entry site of the proton conducting D pathway in the oxidase and involved in inhibition of the oxygen reduction catalysis and proton pumping by internally trapped zinc. Presence of ZnCl2 during liposome reconstitution of cytochrome c oxidase has no effect on the sidedness of the incorporated COX, neither increases the residual amount of soluble COX
Zn2+
-
reaction of enzyme in detergent solution and reconstituted in phospholipid vesicles. At concentrations of Zn2+ below 0.25 mM at the outside of the vesicles, transistion rates between intermediates is not altered. Zn2+ ions bind on both sides of the enzyme and binding at the proton output side selectively impairs proton release during the transition of peroxy intermediate to oxo-ferryl intermediate
Zn2+
-
the Glu-101/His-96 site of subunit II as the site of metal binding inhibits the uptake of protons into the K pathway. Subunit III contributes to zinc binding and/or inhibition of the D pathway
additional information
-
import of COX19 is not inhibited by the ionophore valinomycin indicating that an electrical membrane potential is not required
-
additional information
-
cAMP-dependent tyrosine phosphorylation of subunit I inhibits cytochrome c oxidase activity
-
additional information
-
incubation of the isolated enzyme with protein kinase A, cAMP, and ATP results in serine and threonine phosphorylation of CcO subunit I, which is correlated with sigmoidal inhibition kinetics in the presence of ATP
-
additional information
-
not inhibited by Triton X-100 up to a concentration of 2%
-
additional information
ursodeoxycholateand glycochenodeoxycholate have no observable effect on enzyme activity
-
additional information
-
ursodeoxycholateand glycochenodeoxycholate have no observable effect on enzyme activity
-
additional information
-
high percentage levels of mutated mitochondrial DNA are associated with a dramatic reduction in wild-type levels and COX deficiency. For the m.3243ArG mutation, a superabundance of wild-type mitochondrial DNA is found in many muscle-fiber sections with negligible COX activity
-
additional information
-
knocked down frataxin in oligodendroglioma cells using siRNA produces significant defects in the activity of cytochrome oxidase. Exogenous hemin produces a significant rescue of cytochrome oxidase activity
-
additional information
-
is competitively inhibited early in sepsis and progresses, becoming noncompetitive during the late phase. Exogenous cytochrome c can overcome this myocardial CcOX competitive inhibition. Cecal ligation and puncture inhibit CcOX at 48 h in saline-injected mice. However, cytochrome c injection abrogates this inhibition and restores CcOX kinetic activity to sham values at 48 h
-
additional information
-
CcO immobilized on a metal film
-
additional information
Inactivation of the Aa3 oxidase lead to a 50% reduction in N,N,N',N'-tetramethyl-1,4-benzenediamine (TMPD)-dependent oxidase activity (electron donor specific for cytochrome c-dependent oxidases). Lack of the Cbb3-2 oxidase lead to 65% reduction.; In cells growing exponentially under high oxygen tension (100% air saturation), the absence of ANR lead to a 20fold decrease in mRNA levels of the Cbb3-1 oxidase gene, a decrease that is 10-fold lower than that observed in cells growing exponentially in shaken flasks, and 35-fold lower than in cells entering the stationary phase. When cells are grown under limiting oxygen supply (40% air saturation), the absence of ANR lead to a over 500fold decrease in the mRNA levels of the Cbb3-1 oxidase gene; Under aerobic conditions, inactivation of transcriptional activator gene ANR lead to a significant decrease (more than 230fold) of the mRNA corresponding to the Cbb3-1 oxidase, but have little effect on the other analysed terminal oxidases Cbb3-2 and Aa3.
-
additional information
-
Inactivation of the Aa3 oxidase lead to a 50% reduction in N,N,N',N'-tetramethyl-1,4-benzenediamine (TMPD)-dependent oxidase activity (electron donor specific for cytochrome c-dependent oxidases). Lack of the Cbb3-2 oxidase lead to 65% reduction.; In cells growing exponentially under high oxygen tension (100% air saturation), the absence of ANR lead to a 20fold decrease in mRNA levels of the Cbb3-1 oxidase gene, a decrease that is 10-fold lower than that observed in cells growing exponentially in shaken flasks, and 35-fold lower than in cells entering the stationary phase. When cells are grown under limiting oxygen supply (40% air saturation), the absence of ANR lead to a over 500fold decrease in the mRNA levels of the Cbb3-1 oxidase gene; Under aerobic conditions, inactivation of transcriptional activator gene ANR lead to a significant decrease (more than 230fold) of the mRNA corresponding to the Cbb3-1 oxidase, but have little effect on the other analysed terminal oxidases Cbb3-2 and Aa3.
-
additional information
-
after 30 min of ischemia and 120 min of reperfusion, total COI levels decrease in the left ventricular regions at risk by 72%. Subunit Va is also downregulated by 42% following prolonged ischemia-reperfusion in the left ventricular regions at risk. Cardiac ischemic preconditioning administered before ischemia-reperfusion reduces the loss of COI approximately 30% and prevents COVa losses completely. No losses in subunits Vb and VIIa following ischemia-reperfusion alone, but significant losses occur when cardiac ischemic preconditioning is administered before prolonged ischemia-reperfusion. Delivery of a cell-permeable PKC-epsilon translocation inhibitor to isolated rat hearts before prolonged ischemia-reperfusion dramatically increases COI loss
-
additional information
-
CCO activity, the content of the mitochondrial-encoded CCO subunit 1 (COX1), and the content of the nuclear-encoded subunit COX4 in cardiac mitochondria are reduced in 21-d-old offspring of Cu-deficient dams. COX1 content is normal in 21-d-old cross-fostered offspring of Cu-deficient dams, but CCO activity and COX4 are reduced
-
additional information
-
rapid isolation of mitochondria from rat heart in the presence of various protein phosphatase inhibitors (in the presence of 25 mM NaF, 5 mM sodium vanadate, 10 nM okadaic acid, 2 mM EGTA, and 0.2% bovine serum albumin) results in CcO kinetics with allosteric ATP-inhibition and phosphorylation of subunit I at serine, threonine, and tyrosine
-
additional information
-
enzyme activity decreases only at the late stage of diabetes which is not normalized by insulin treatment. Activity at room temperature (25°C) as well as at physiological temperature (37°C) is not affected by the diabetic state. At the late stage of diabetes the activity at 37°C decreases by 22%
-
additional information
-
ethanol withdrawal decreases the activity of total COX, COX I, and COX IV. Estrogen treatment (17beta-estradiol) prevents the effects of withdrawal on the activities of total COX and COX IV but not COX I. Neither withdrawal nor 17beta-estradiol alter the protein levels of the subunits
-
additional information
-
15 min of global ischemia leads to the inhibition of COXI synthesis to 56% of control. After 1, 3 and 24 hours of reperfusion, COXI synthesis is inhibited to 46, 50 and 72% of control, respectively. Extent COXIII and COXII/ATPase6 synthesis inhibition is comparable to the extent of COXI synthesis inhibition. No significant changes in COXI mRNA and in both COXI and COXII protein level after ischemia, thus ischemia-reperfusion affects directly mitochondrial translation machinery. Ischemia in duration of 15 min and consequent 1, 3 and 24 hours of reperfusion leads to the inhibition of COX activity to 90.3, 80.3, 81.9 and 83.5% of control, respectively
-
additional information
-
rats exposed to a GSM signal at 6W/Kg show decreased CO activity in some areas of the prefrontal and frontal cortex (infralimbic cortex, prelimbic cortex, primary motor cortex, secondary motor cortex, anterior cingulate cortex areas 1 and 2), the septum (dorsal and ventral parts of the lateral septal nucleus), the hippocampus (dorsal field CA1, CA2 and CA3 of the hippocampus and dental gyrus) and the posterior cortex (retrosplenial agranular cortex, primary and secondary visual cortex, perirhinal cortex and lateral entorhinal cortex). Exposure to GSM at 1.5W/Kg does not affect brain activity
-
additional information
the enzyme is resistant to specific inhibitors of copper-containing oxidases, such as NaN3 and NaF
-
additional information
-
the enzyme is resistant to specific inhibitors of copper-containing oxidases, such as NaN3 and NaF
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00002 - 0.13
ferrocytochrome c
0.0047 - 0.0065
ferrocytochrome c549
-
0.003 - 0.024
ferrocytochrome c550
-
0.067
ferrocytochrome c551
-
0.002 - 0.018
ferrocytochrome c552
-
0.0009
ferrocytochrome c553
-
-
0.86
N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
0.09
o-Dianisidine
-
at 1 mM H2O2
0.23 - 0.27
reduced ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine
-
2
reduced ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine
-
-
-
0.000023 - 0.000154
reduced cytochrome c551
-
additional information
additional information
-
0.00002
ferrocytochrome c
-
biphasic kinetic with 2 different Km values
0.00005
ferrocytochrome c
-
high affinity Km, kidney, heart, and muscle enzyme, at 27 mM ionic strength
0.00005
ferrocytochrome c
-
high-affinity Km
0.00006
ferrocytochrome c
-
biphasic kinetic, high-affinity phase Km
0.00007
ferrocytochrome c
-
high affinity Km, liver enzyme, at 27 mM ionic strength
0.00012
ferrocytochrome c
-
heart enzyme, high affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid
0.00016
ferrocytochrome c
-
liver enzyme, high affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid
0.00071
ferrocytochrome c
-
heart enzyme, low affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid
0.00126
ferrocytochrome c
-
2 Km values for horse heart, Neurospora crassa, Saccharomyces cerevisiea and Candida krusei cytochrome c
0.0013
ferrocytochrome c
-
horse heart cytochrome c, chymotrypsin treated enzyme
0.00132
ferrocytochrome c
-
horse heart cytochrome c, high-affinity Km, 30 mM ionic strength
0.0014
ferrocytochrome c
-
horse heart cytochrome c
0.00148
ferrocytochrome c
-
liver enzyme, low affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid
0.0017
ferrocytochrome c
-
horse cytochrome c, presence of cardiolipin
0.0017
ferrocytochrome c
-
horse heart cytochrome c, in the presence of 0.1% Triton X-100 and 2 mg/ml asolectin, chymotrypsin treated enzyme
0.0018
ferrocytochrome c
-
horse cytochrome c, in the presence of cardiolipin
0.002
ferrocytochrome c
-
-
0.002
ferrocytochrome c
-
yeast cytochrome c
0.002
ferrocytochrome c
-
Saccharomyces cerevisiae cytochrome c
0.002
ferrocytochrome c
-
low-affinity Km
0.0021
ferrocytochrome c
-
horse heart cytochrome c, in the presence of 0.1% Triton X-100 and 2 mg/ml asolectin
0.0036
ferrocytochrome c
-
enzyme from swayback-diseased liver, low-affinity Km
0.0037
ferrocytochrome c
-
-
0.0037
ferrocytochrome c
-
Candida krusei cytochrome c
0.0037
ferrocytochrome c
-
Candida krusei cytochrome c, in the presence of cardiolipin
0.0038
ferrocytochrome c
-
horse cytochrome c, in the presence of cardiolipin
0.004
ferrocytochrome c
-
horse cytochrome c, in dodecylmaltoside
0.004
ferrocytochrome c
-
biphasic kinetic with 2 different Km values
0.0042
ferrocytochrome c
-
biphasic kinetic, low-affinity phase Km
0.0045
ferrocytochrome c
-
yeast cytochrome c
0.0047
ferrocytochrome c
-
enzyme from swayback-diseased brain, low-affinity Km
0.0055
ferrocytochrome c
-
horse heart cytochrome c
0.0058
ferrocytochrome c
-
enzyme from normal liver, high-affinity Km
0.006 - 0.077
ferrocytochrome c
-
dependency on pH, phosphate and K+ concentration
0.0067
ferrocytochrome c
-
-
0.0067
ferrocytochrome c
-
Saccharomyces cerevisiae cytochrome c
0.0067
ferrocytochrome c
-
enzyme from normal liver, low-affinity Km
0.008
ferrocytochrome c
-
low affinity Km, liver enzyme at 27 mM ionic strength
0.0081
ferrocytochrome c
-
horse cytochrome c
0.0087
ferrocytochrome c
-
Candida krusei cytochrome c
0.009
ferrocytochrome c
-
reduced horse heart cytochrome
0.01
ferrocytochrome c
-
yeast cytochrome c, approx. value
0.01 - 0.015
ferrocytochrome c
-
-
0.011
ferrocytochrome c
-
-
0.011
ferrocytochrome c
-
-
0.011
ferrocytochrome c
-
horse heart cytochrome c
0.011
ferrocytochrome c
-
horse cytochrome c
0.011
ferrocytochrome c
-
low affinity Km, muscle enzyme at 27 mM ionic strength
0.012
ferrocytochrome c
-
horse cytochrome c, absence of cardiolipin
0.012
ferrocytochrome c
-
horse heart cytochrome c
0.012
ferrocytochrome c
-
low affinity Km, kidney enzyme at 27 mM ionic strength
0.012
ferrocytochrome c
-
enzyme from normal brain, low-affinity Km
0.012
ferrocytochrome c
-
enzyme from swayback-diseased liver, high-affinity Km
0.013
ferrocytochrome c
-
Thermus thermophilus cytochrome c
0.015
ferrocytochrome c
-
horse heart cytochrome c
0.015
ferrocytochrome c
-
low affinity Km, heart enzyme at 27 mM ionic strength
0.015
ferrocytochrome c
-
yeast cytochrome c, in the presence of 100 mM KCl
0.0153
ferrocytochrome c
-
horse heart cytochrome c, 100 mM ionic strength
0.016
ferrocytochrome c
-
Candida krusei cytochrome c
0.016
ferrocytochrome c
-
horse heart cytochrome c, in the presence of 50 mM KCl
0.017
ferrocytochrome c
-
kidney enzyme, 226 mM ionic strength
0.019
ferrocytochrome c
-
Candida krusei cytochrome c
0.019
ferrocytochrome c
-
oxidation of horse cytochrome c
0.022
ferrocytochrome c
-
liver enzyme, 226 mM ionic strength
0.023
ferrocytochrome c
-
heart enzyme, 226 mM ionic strength
0.024
ferrocytochrome c
-
horse cytochrome c
0.025
ferrocytochrome c
-
muscle enzyme, 226 mM ionic strength
0.025
ferrocytochrome c
-
adult heart enzyme
0.026
ferrocytochrome c
-
oxidation of bovine or yeast cytochrome c
0.027
ferrocytochrome c
-
Candida krusei cytochrome c
0.029
ferrocytochrome c
-
Saccharomyces oviformis cytochrome c
0.031
ferrocytochrome c
-
Nitrosomonas europaea cytochrome c
0.032 - 0.044
ferrocytochrome c
-
-
0.0355
ferrocytochrome c
-
28°C, pH not specified in the publication
0.037
ferrocytochrome c
-
following sham exposure
0.038
ferrocytochrome c
-
fetal heart enzyme
0.0407
ferrocytochrome c
-
28°C, presence of 3 mM ADP, pH not specified in the publication
0.041
ferrocytochrome c
-
horse cytochrome c
0.041
ferrocytochrome c
-
following CO exposure
0.05
ferrocytochrome c
-
horse and native cytochrome c
0.053
ferrocytochrome c
-
tuna cytochrome c
0.055
ferrocytochrome c
-
enzyme from normal brain, high-affinity Km
0.06
ferrocytochrome c
-
-
0.06
ferrocytochrome c
-
-
0.06
ferrocytochrome c
-
-
0.067
ferrocytochrome c
-
Saccharomyces cerevisiae cytochrome c
0.074
ferrocytochrome c
-
Candida krusei cytochrome c
0.11
ferrocytochrome c
-
horse cytochrome c
0.12
ferrocytochrome c
-
cow cytochrome c
0.13
ferrocytochrome c
-
from horse heart, bacterial enzyme
0.13
ferrocytochrome c
-
horse heart cytochrome c
0.13
ferrocytochrome c
-
hose cytochrome c
0.13
ferrocytochrome c
-
horse heart cytochrome c, low-affinity Km, 30 mM ionic strength
0.0047
ferrocytochrome c549
-
Candida krusei cytochrome c
-
0.0065
ferrocytochrome c549
-
-
-
0.003
ferrocytochrome c550
-
Magnetospirillum magnetotacticum cytochrome c550
-
0.008
ferrocytochrome c550
-
-
-
0.024
ferrocytochrome c550
-
-
-
0.067
ferrocytochrome c551
-
from thermophilic bacterium PS3, bacterial enzyme
-
0.067
ferrocytochrome c551
-
cytochrome c551 from thermophilic bacterium PS3
-
0.002 - 0.003
ferrocytochrome c552
-
-
-
0.0022
ferrocytochrome c552
-
-
-
0.0043
ferrocytochrome c552
-
-
-
0.0093
ferrocytochrome c552
-
at pH 3.5
-
0.011
ferrocytochrome c552
-
from Thermus thermophilus, bacterial enzyme
-
0.011
ferrocytochrome c552
-
cytochrome c552 from Thermus thermophilus
-
0.016
ferrocytochrome c552
-
-
-
0.018
ferrocytochrome c552
-
-
-
0.00004
O2
-
-
0.23
reduced ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine
-
-
-
0.27
reduced ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine
-
-
-
0.000023
reduced cytochrome c551
-
mutant enzyme E116Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000026
reduced cytochrome c551
-
wild type enzyme, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000035
reduced cytochrome c551
-
mutant enzyme E84Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000044
reduced cytochrome c551
-
mutant enzyme D49N, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000059
reduced cytochrome c551
-
mutant enzyme E66Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000063
reduced cytochrome c551
-
mutant enzyme E139Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000074
reduced cytochrome c551
-
mutant enzyme E68Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.0001
reduced cytochrome c551
-
mutant enzyme E64Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000154
reduced cytochrome c551
-
mutant enzyme D99N, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
additional information
additional information
-
enzyme exhibits positive cooperativity at low ionic strength, increasing the KCl concentration to 25 mM causes loss of cooperativity
-
additional information
additional information
-
comparison of high and low affinity Km values at low ionic strength with Rhodobacter spaeroides and horse cytochrome c of wild-type and various mutants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
50 - 100
cytochrome c
-
soluble enzyme, higher values for particulate enzyme
15.3
diaminodurene
-
ascorbate/diaminodurene assay system
0.57 - 2000
ferrocytochrome c
8
ferrocytochrome c549
-
-
-
1.3 - 37.4
ferrocytochrome c550
-
4 - 9.78
ferrocytochrome c552
-
252
ferrocytochrome c553
-
-
3.93 - 220
N,N,N',N'-tetramethyl-4-phenylendiamine
-
24.3
phenazine methosulfate
-
ascorbate/phenazine methosulfate assay system
30 - 325
reduced cytochrome c551
-
additional information
additional information
-
0.57
ferrocytochrome c
-
horse cytochrome c
1
ferrocytochrome c
-
at 7°C, in presence of 56% ethylene glycol
1.6
ferrocytochrome c
-
Candida krusei cytochrome c
1.8
ferrocytochrome c
-
Nitrosomonaseuropaea cytochrome c
2.08 - 2.58
ferrocytochrome c
-
-
3.88
ferrocytochrome c
-
horse cytochrome c
4 - 5
ferrocytochrome c
-
Saccharomyces cerevisiae cytochrome c, in the presence of 0.05% laurylmaltoside
5 - 7
ferrocytochrome c
-
Saccharomyces cerevisiae cytochrome c, in the presence of asolectin
6
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, W143A mutant enzyme
8 - 12
ferrocytochrome c
-
in the presence of 0.1% dodecyl-beta-D-maltoside
8.33
ferrocytochrome c
-
Candida krusei cytochrome c
9.38
ferrocytochrome c
-
horse heart cytochrome c
11 - 30
ferrocytochrome c
-
oxidation of horse heart cytochrome c
12
ferrocytochrome c
-
at 7°C in absence of ethylene glycol
13.3 - 16
ferrocytochrome c
-
enzyme reconstituted into asolectin liposomes
14
ferrocytochrome c
-
Candida krusei cytochrome c, in the presence of cardiolipin
20
ferrocytochrome c
-
Thiobacillus novellus cytochrome c, 12.5 mM phosphate at pH 5.5 and 20°C
20
ferrocytochrome c
-
horse cytochrome c, W143A mutant enzyme
20
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, W143F mutant enzyme
20
ferrocytochrome c
-
R54M mutant enzyme
24
ferrocytochrome c
-
Candida krusei cytochrome c
30
ferrocytochrome c
-
high-affinity reaction
30 - 600
ferrocytochrome c
-
-
30 - 600
ferrocytochrome c
-
-
32
ferrocytochrome c
-
horse cytochrome c
32
ferrocytochrome c
-
horse cytochrome c, in the presence of cardiolipin
36
ferrocytochrome c
-
oxidation of horse heart cytochrome c
40
ferrocytochrome c
-
horse cytochrome c, W143F mutant enzyme
45.8
ferrocytochrome c
-
Candida krusei cytochrome c, 30 mM phosphate at pH 5.5 and 20°C
50
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, D229N mutant enzyme
50 - 100
ferrocytochrome c
-
soluble enzyme, higher values for particulate enzyme
50 - 100
ferrocytochrome c
-
soluble enzyme, higher values for particulate enzyme
53
ferrocytochrome c
-
Thermus thermophilus cytochrome c
54
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, D195Q mutant enzyme
66
ferrocytochrome c
-
horse heart cytochrome c
80
ferrocytochrome c
-
horse cytochrome c
80
ferrocytochrome c
-
low-affinity reaction
90
ferrocytochrome c
-
horse-heart cytochrome c
90
ferrocytochrome c
-
cow cytochrome c
100
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, E157Q and E254A mutant enzyme
111
ferrocytochrome c
-
Crithidia fasciculata cytochrome c, very low turnover numbers with human, yeast, rat, horse, and bovine cytochrome c
120
ferrocytochrome c
-
fetal heart enzyme
133
ferrocytochrome c
-
-
158
ferrocytochrome c
-
horse cytochrome c
160
ferrocytochrome c
-
Saccharomyces oviformis cytochrome c
180
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, D214N mutant enzyme
187
ferrocytochrome c
-
horse heart cytochrome c
200
ferrocytochrome c
-
adult heart enzyme
220
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, D151N/E152Q mutant enzyme
230
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, E148Q mutant enzyme
260
ferrocytochrome c
-
tuna cytochrome c
260
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, D188N/E189Q mutant enzyme
270
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, wild-type enzyme
290
ferrocytochrome c
-
Candida krusei cytochrome c
290
ferrocytochrome c
-
wild-type enzyme, horse cytochrome c, 155 mM ionic strength
300
ferrocytochrome c
-
-
300
ferrocytochrome c
-
horse heart cytochrome c
336
ferrocytochrome c
-
horse cytochrome c, in the presence of cardiolipin
350
ferrocytochrome c
-
muscle enzyme
360
ferrocytochrome c
-
muscle enzyme
380
ferrocytochrome c
-
heart enzyme
400
ferrocytochrome c
-
horse cytochrome c, D214N and D229N mutant enzyme
400 - 500
ferrocytochrome c
-
-
410
ferrocytochrome c
-
muscle enzyme
500
ferrocytochrome c
-
enzyme from kidney, photometric assay
520
ferrocytochrome c
-
enzyme from diaphragm, photometric assay
535
ferrocytochrome c
-
purified COV
540
ferrocytochrome c
-
enzyme from liver, photometric assay
550
ferrocytochrome c
-
enzyme from heart, photometric assay
550
ferrocytochrome c
-
reconstituted recombinant D407C mutant enzyme
590
ferrocytochrome c
-
wild-type enzyme, horse cytochrome c, 5 mM ionic strength
600
ferrocytochrome c
-
horse cytochrome c, E157Q and E254Amutant enzyme
650
ferrocytochrome c
-
recombinant D407C mutant enzyme
700
ferrocytochrome c
-
reconstituted recombinant D407A mutant enzyme
700
ferrocytochrome c
-
reconstituted recombinant D407N mutant enzyme
708
ferrocytochrome c
-
unpurified COV
980
ferrocytochrome c
-
wild-type, D188N/E189Q and D151N/E152Q mutant enzyme, horse cytochrome c, 75 mM ionic strength
1000
ferrocytochrome c
-
-
1100
ferrocytochrome c
-
recombinant D407A mutant enzyme
1100
ferrocytochrome c
-
horse cytochrome c, E148Q mutant enzyme
1200
ferrocytochrome c
-
reconstituted wild-type enzyme
1200
ferrocytochrome c
-
horse cytochrome c, D195Q mutant enzyme
1300
ferrocytochrome c
-
wild-type enzyme
1300
ferrocytochrome c
-
horse cytochrome c, D151N/E152Q mutant enzyme
1400
ferrocytochrome c
-
recombinant D407N mutant enzyme
1500
ferrocytochrome c
-
horse heart cytochrome c
1600
ferrocytochrome c
-
horse cytochrome c, D188N/E189Q mutant enzyme
1700
ferrocytochrome c
-
horse cytochrome c, wild-type enzyme
2000
ferrocytochrome c
-
recombinant enzyme
1.3
ferrocytochrome c550
-
-
-
37.4
ferrocytochrome c550
-
Magnetospirillum magnetotacticum cytochrome c550
-
4
ferrocytochrome c552
-
-
-
9.78
ferrocytochrome c552
-
-
-
3.93
N,N,N',N'-tetramethyl-4-phenylendiamine
-
ascorbate/N,N,N',N'-tetramethyl-p-phenylendiamine assay system
-
7.5
N,N,N',N'-tetramethyl-4-phenylendiamine
-
-
-
60
N,N,N',N'-tetramethyl-4-phenylendiamine
-
ascorbate/N,N,N',N'-tetramethyl-p-phenylendiamine assay system
-
180
N,N,N',N'-tetramethyl-4-phenylendiamine
-
-
-
220
N,N,N',N'-tetramethyl-4-phenylendiamine
-
-
-
30
reduced cytochrome c551
-
mutant enzyme E116Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
140
reduced cytochrome c551
-
mutant enzyme D99N, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
199
reduced cytochrome c551
-
mutant enzyme E66Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
200
reduced cytochrome c551
-
mutant enzyme D49N, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
290
reduced cytochrome c551
-
mutant enzyme E68Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
295
reduced cytochrome c551
-
wild type enzyme, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
297
reduced cytochrome c551
-
mutant enzyme E139Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
317
reduced cytochrome c551
-
mutant enzyme E64Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
325
reduced cytochrome c551
-
mutant enzyme E84Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
additional information
additional information
-
kcat increases with decreasing pH
-
additional information
additional information
-
above 20 mM phosphate: rapid decrease of kcat with Candida krusei, tuna, Thiobacillus novellus, and horse cytochrome c
-
additional information
additional information
-
highest turnover number at 55 mM ionic strength: D214N, D195N and E148Q, highest turnover number at 45 mM ionic strength: E157Q, comparison of high and low affinity turnover numbers at low ionic strength with Rhodobacter spaeroides and horse cytochrome c of wild-type and various mutants
-
additional information
additional information
-
study of reaction kinetics assuming a fast protonic phase with a proton transfer to H291 and a slow process with a proton transfer to OH-group of binuclear catalytic site. Comparison with kinetics of enzyme from Paracoccus denitrificans and Bos taurus
-
additional information
additional information
-
study of reaction kinetics assuming a fast protonic phase with a proton transfer to H291 and a slow process with a proton transfer to OH-group of binuclear catalytic site. Comparison with kinetics of enzyme from Rhodobacter spaeroides and Bos taurus
-
additional information
additional information
-
study of reaction kinetics assuming a fast protonic phase with a proton transfer to H291 and a slow process with a proton transfer to OH-group of binuclear catalytic site. Comparison with kinetics of enzyme from Rhodobacter spaeroides and Paracoccus denitrificans
-
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10000
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
10068
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
10670
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
11000
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
114000
-
analytical ultracentrifugation
11500
-
1 * 29000, 1 * 21000, 1 * 11500, 1 * 9500, SDS-PAGE
11600
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
12000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
12200
-
x * 30500 + x * 25500 + x * 12200 + x * 9500, SDS-PAGE
12233
-
x * 12233, MALDI-TOF, x * 12236, calculated
12236
-
x * 12233, MALDI-TOF, x * 12236, calculated
12436
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
12627
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
12723
-
x * 12723, MALDI-TOF, x * 12724, calculated
12724
-
x * 12723, MALDI-TOF, x * 12724, calculated
13700
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
14570
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
14858
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
158000
-
sedimentation equilibrium, monomeric enzyme complex
162000
-
calculation from heme content
170000
-
nondenaturing PAGE
17074
-
1 * 60371 + 1 * 17074 + 1 * 5976, calculated from amino acid sequence
17153
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
17500
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
17900
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
180000 - 280000
-
minimal molecular weight, calculated from subunit composition, heme content
190000 - 225000
-
sucrose density gradient centrifugation
20000
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
20100
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
204000
-
amino acid sequence of 12 subunits + 6000 Da for subunit VIIb
22400
-
1 * 54950 + 1 * 27850 + 1 * 22400, SDS-PAGE
226000
-
estimated from sucrose density gradient centrifugation and gel filtration
23100
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
23470
-
1 * 58360 + 1 * 34840 + 1 * 23470, MALDI-TOF mass spectrometry
250000
-
gel filtration in the presence of N-lauryl sarcosinate
25500
-
x * 30500 + x * 25500 + x * 12200 + x * 9500, SDS-PAGE
26049
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
26678
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
27000
-
1 * 40000 + 1 * 27000, SDS-PAGE
27850
-
1 * 54950 + 1 * 27850 + 1 * 22400, SDS-PAGE
29500
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
29918
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
30340
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
30500
-
x * 30500 + x * 25500 + x * 12200 + x * 9500, SDS-PAGE
326000
-
dimeric enzyme complex, sedimentation equilibrium centrifugation
33500
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
34300
-
1 * 71600 + 1 * 34300, densitometric scan
34840
-
1 * 58360 + 1 * 34840 + 1 * 23470, MALDI-TOF mass spectrometry
350000
-
dimeric form, Triton X-100 solubilized, hydrodynamic measurements
35100
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
36000
-
1 * 48000-49000 + 1 * 36000, SDS-PAGE, immunoblotting
41000
-
1 * 41000 + 1 * 35000 + 1 * 26000, SDS-PAGE
43600
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
47000
-
x * 47000 + x * 31000 + x * 19000, SDS-PAGE
51000
-
1 * 51000 + 1 * 31000, SDS-PAGE, Ferguson plot
52000
-
1 * 52000 + 1 * 37000 + 1 * 29000, SDS-PAGE
5364
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
54000
-
1 * 54000 + 1 * 32000, SDS-PAGE
5441
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
5444
Cox7c, mass spectrometry
54950
-
1 * 54950 + 1 * 27850 + 1 * 22400, SDS-PAGE
5600
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
56400
-
sequence analysis
56993
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
58000
-
1 * 58000 + 1 * 26000, 58000 Da band may be composed of 2 subunits of the cb-type oxidase, the 26000 Da subunit may be a heme c bearing diheme or mono-heme of the enzyme, SDS-PAGE
58360
-
1 * 58360 + 1 * 34840 + 1 * 23470, MALDI-TOF mass spectrometry
5976
-
1 * 60371 + 1 * 17074 + 1 * 5976, calculated from amino acid sequence
6000
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
60371
-
1 * 60371 + 1 * 17074 + 1 * 5976, calculated from amino acid sequence
6244
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
6303
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
6350
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
65000
-
1 * 65000, b heme
6603
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
67000
-
calculation from heme content
71600
-
1 * 71600 + 1 * 34300, densitometric scan
79000
-
SDS-PAGE, no mercaptoethanol
82000
-
1 * 38000, 1 * 57000, 1 * 82000
83000
-
calculation from heme content
8480
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
86000
-
sedimentation analysis
8750
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
8800
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
88000 - 90000
gel filtration
9000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
92000
-
SDS-PAGE, no mercaptoethanol
9419
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
115000
-
-
115000
-
sedimentation analysis
13000
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
13000
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
14000
-
1 * 56000 + 1 * 40000 + 1 * 14000, SDS-PAGE
14000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
140000 - 158000
-
-
140000 - 158000
-
calculation from heme content
140000 - 158000
-
sedimentation equilibrium analysis, monomeric form
18000
Cox4, immunoblot analysis
18000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
19000
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
19000
-
x * 47000 + x * 31000 + x * 19000, SDS-PAGE
200000
-
gel filtration
200000
-
heart, monomeric enzyme, deoxycholate solubilized, hydrodynamic measurements
21000
-
1 * 57000 + 1 * 37000 + 1 * 21000, SDS-PAGE
21000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
21000
-
1 * 29000, 1 * 21000, 1 * 11500, 1 * 9500, SDS-PAGE
210000
gel filtration
210000
-
vertebrate, theoretical value of monomer composed of 12-13 different subunits
22000
-
1 * 56000 + 1 * 38000 + 1 * 22000, SDS-PAGE, Ferguson plot
22000
-
1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE
22000
-
1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE
23000
-
1 * 23000 + 1 * 32000, SDS-PAGE
23000
-
1 * 45000 + 1 * 28000 + 1 * 23000, SDS-PAGE
23000
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
23000
-
x * 32000 + x * 23000, SDS-PAGE
26000
-
1 * 58000 + 1 * 26000, 58000 Da band may be composed of 2 subunits of the cb-type oxidase, the 26000 Da subunit may be a heme c bearing diheme or mono-heme of the enzyme, SDS-PAGE
26000
-
1 * 41000 + 1 * 35000 + 1 * 26000, SDS-PAGE
26000
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
28000
-
1 * 39000 + 1 * 28000, SDS-PAGE
28000
-
1 * 45000 + 1 * 28000, SDS-PAGE
28000
-
1 * 43000 + 1 * 34000 + 1 * 28000, SDS-PAGE, 5% 2-mercaptoethanol
28000
-
1 * 45000 + 1 * 28000 + 1 * 23000, SDS-PAGE
28000
-
x * 39000 + x * 28000, SDS-PAGE
29000
-
1 * 52000 + 1 * 37000 + 1 * 29000, SDS-PAGE
29000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
29000
-
1 * 29000, 1 * 21000, 1 * 11500, 1 * 9500, SDS-PAGE
290000 - 315000
-
enzyme associated with detergents
290000 - 315000
-
gel filtration, value depending on ionic strength
30000
-
1 * 30000 + 1 * 50000, SDS-PAGE
30000
-
x * 50000 + x * 30000, SDS-PAGE
31000
-
1 * 51000 + 1 * 31000, SDS-PAGE, Ferguson plot
31000
-
x * 47000 + x * 31000 + x * 19000, SDS-PAGE
32000
-
1 * 55000 + 1 * 32000, SDS-PAGE
32000
-
1 * 55000 + 1 * 32000, SDS-PAGE, immunoblotting
32000
-
1 * 54000 + 1 * 32000, SDS-PAGE
32000
-
1 * 23000 + 1 * 32000, SDS-PAGE
32000
-
x * 32000 + x * 23000, SDS-PAGE
33000
-
1 * 50000 + 1 * 33000, SDS-PAGE
33000
-
1 * 55000 or 71000 + 1 * 33000, SDS-PAGE
33000
-
1 * 55000 + 1 * 33000, SDS-PAGE
34000
-
1 * 71000 + 1 * 34000, subunit I shows anomalous behaviour on SDS-PAGE, Ferguson plot
34000
-
1 * 43000 + 1 * 34000 + 1 * 28000, SDS-PAGE, 5% 2-mercaptoethanol
34000
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
35000
Cox1, immunoblot analysis
35000
-
1 * 41000 + 1 * 35000 + 1 * 26000, SDS-PAGE
35000
-
1 * 35000 + 1 * 37000 + 1 * 45000, SDS-PAGE
35000
-
x * 45000 + x * 37000 + x * 35000, SDS-PAGE
37000
-
1 * 52000 + 1 * 37000 + 1 * 29000, SDS-PAGE
37000
-
1 * 35000 + 1 * 37000 + 1 * 45000, SDS-PAGE
37000
-
1 * 57000 + 1 * 37000 + 1 * 21000, SDS-PAGE
37000
-
1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE
37000
-
1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE
37000
-
x * 45000 + x * 37000 + x * 35000, SDS-PAGE
38000
-
1 * 56000 + 1 * 38000 + 1 * 22000, SDS-PAGE, Ferguson plot
38000
-
1 * 38000, 1 * 57000, 1 * 82000
39000
-
1 * 39000 + 1 * 28000, SDS-PAGE
39000
-
x * 39000 + x * 28000, SDS-PAGE
39000
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
40000
-
1 * 40000 + 1 * 27000, SDS-PAGE
40000
-
1 * 56000 + 1 * 40000 + 1 * 14000, SDS-PAGE
40000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
43000
-
2 * 43000, SDS-PAGE, 0.5% 2-mercaptoethanol
43000
-
1 * 43000 + 1 * 34000 + 1 * 28000, SDS-PAGE, 5% 2-mercaptoethanol
45000
-
1 * 45000 + 1 * 28000, SDS-PAGE
45000
-
1 * 45000 + 1 * 28000 + 1 * 23000, SDS-PAGE
45000
-
1 * 35000 + 1 * 37000 + 1 * 45000, SDS-PAGE
45000
-
x * 45000 + x * 37000 + x * 35000, SDS-PAGE
50000
-
1 * 50000 + 1 * 33000, SDS-PAGE
50000
-
1 * 30000 + 1 * 50000, SDS-PAGE
50000
-
x * 50000 + x * 30000, SDS-PAGE
55000
-
1 * 55000 + 1 * 32000, SDS-PAGE
55000
-
1 * 55000 + 1 * 32000, SDS-PAGE, immunoblotting
55000
-
1 * 55000 or 71000 + 1 * 33000, SDS-PAGE
55000
-
1 * 55000 + 1 * 33000, SDS-PAGE
55000
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
56000
-
1 * 56000 + 1 * 40000 + 1 * 14000, SDS-PAGE
56000
-
1 * 56000 + 1 * 38000 + 1 * 22000, SDS-PAGE, Ferguson plot
56000
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
5700
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
5700
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
57000
-
1 * 57000 + 1 * 37000 + 1 * 21000, SDS-PAGE
57000
-
1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE
57000
-
1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE
57000
-
1 * 38000, 1 * 57000, 1 * 82000
71000
-
calculated
71000
-
1 * 71000 + 1 * 34000, subunit I shows anomalous behaviour on SDS-PAGE, Ferguson plot
9500
-
x * 30500 + x * 25500 + x * 12200 + x * 9500, SDS-PAGE
9500
-
1 * 29000, 1 * 21000, 1 * 11500, 1 * 9500, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 12723, MALDI-TOF, x * 12724, calculated
?
-
x * 45000 + x * 37000 + x * 35000, SDS-PAGE
?
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
?
-
x * 12233, MALDI-TOF, x * 12236, calculated
?
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
?
-
x * 47000 + x * 31000 + x * 19000, SDS-PAGE
?
-
x * 39000 + x * 28000, SDS-PAGE
?
-
x * 50000 + x * 30000, SDS-PAGE
?
-
x * 50000 + x * 30000, SDS-PAGE
-
?
-
x * 42000 + x * 36000 + x * 24000, SDS-PAGE
?
-
x * 42000 + x * 36000 + x * 24000, SDS-PAGE
-
?
-
x * 30500 + x * 25500 + x * 12200 + x * 9500, SDS-PAGE
?
-
x * 32000 + x * 23000, SDS-PAGE
dimer
-
-
dimer
-
1 * 71600 + 1 * 34300, densitometric scan
dimer
-
2 * 43000, SDS-PAGE, 0.5% 2-mercaptoethanol
dimer
-
1 * 58000 + 1 * 26000, 58000 Da band may be composed of 2 subunits of the cb-type oxidase, the 26000 Da subunit may be a heme c bearing diheme or mono-heme of the enzyme, SDS-PAGE
dimer
-
1 * 49000-50000 + 1 * 42000-43000, SDS-PAGE, immunoblotting
dimer
-
1 * 54000 + 1 * 32000, SDS-PAGE
dimer
-
1 * 51000 + 1 * 31000, SDS-PAGE, Ferguson plot
dimer
-
1 * 40000 + 1 * 27000, SDS-PAGE
dimer
-
1 * 39000 + 1 * 28000, SDS-PAGE
dimer
-
1 * 50000 + 1 * 33000, SDS-PAGE
dimer
-
2 subunits, analogous to subunits I and II of eukaryotes
dimer
-
1 * 45000 + 1 * 28000, SDS-PAGE
dimer
-
1 * 30000 + 1 * 50000, SDS-PAGE
dimer
-
1 * 30000 + 1 * 50000, SDS-PAGE
-
dimer
-
CuCox19 and apoCox19, sedimentation equilibrium
dimer
-
CuCox19 and apoCox19, sedimentation equilibrium
-
dimer
-
1 * 23000 + 1 * 32000, SDS-PAGE
dimer
-
1 * 55000 + 1 * 32000, SDS-PAGE
dimer
-
1 * 55000 + 1 * 32000, SDS-PAGE, immunoblotting
dimer
-
1 * 46000-55000 + 1 * 29000-32000, SDS-PAGE, immunoblotting
dimer
-
1 * 22000-26000 + 1 * 14000-17000, SDS-PAGE, immunoblotting
dimer
-
1 * 55000 or 71000 + 1 * 33000, SDS-PAGE
dimer
-
1 * 71000 + 1 * 34000, subunit I shows anomalous behaviour on SDS-PAGE, Ferguson plot
dimer
-
1 * 55000 + 1 * 33000, SDS-PAGE
dimer
-
1 * 55000 or 71000 + 1 * 33000, SDS-PAGE
-
dimer
-
1 * 48000-49000 + 1 * 36000, SDS-PAGE, immunoblotting
heterotrimer
-
1 * 60371 + 1 * 17074 + 1 * 5976, calculated from amino acid sequence
heterotrimer
-
1 * 60371 + 1 * 17074 + 1 * 5976, calculated from amino acid sequence
-
homodimer
-
2 * 35000, SDS-PAGE
homotrimer
3 * 33900, calculated from sequence
homotrimer
3 * 39000, SDS-PAGE after boiling
homotrimer
-
3 * 33900, calculated from sequence
-
homotrimer
-
3 * 39000, SDS-PAGE after boiling
-
monomer
1 210000, calculated from sequence
monomer
-
1 * 65000, b heme
oligomer
-
-
oligomer
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
oligomer
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
oligomer
-
mitochondrial COX consists of up to 13 subunits
oligomer
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
oligomer
-
cytochrome c oxidase is composed by 13 subunits
oligomer
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
oligomer
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
oligomer
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
tetramer
-
1 * 29000, 1 * 21000, 1 * 11500, 1 * 9500, SDS-PAGE
tetramer
-
1 * 29000, 1 * 21000, 1 * 11500, 1 * 9500, SDS-PAGE
-
trimer
-
1 * 54950 + 1 * 27850 + 1 * 22400, SDS-PAGE
trimer
-
1 * 56000 + 1 * 38000 + 1 * 22000, SDS-PAGE, Ferguson plot
trimer
-
1 * 57000 + 1 * 37000 + 1 * 21000, SDS-PAGE
trimer
-
1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE
trimer
-
1 * 57000 + 1 * 37000 + 1 * 21000, SDS-PAGE
-
trimer
-
1 * 35000 + 1 * 37000 + 1 * 45000, SDS-PAGE
trimer
-
1 * 56000 + 1 * 40000 + 1 * 14000, SDS-PAGE
trimer
-
1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE
trimer
-
1 * 43000 + 1 * 34000 + 1 * 28000, SDS-PAGE, 5% 2-mercaptoethanol
trimer
-
1 * 45000 + 1 * 28000 + 1 * 23000, SDS-PAGE
trimer
-
1 * 38000, 1 * 57000, 1 * 82000
trimer
-
1 * 58360 + 1 * 34840 + 1 * 23470, MALDI-TOF mass spectrometry
trimer
-
1 * 41000 + 1 * 35000 + 1 * 26000, SDS-PAGE
trimer
-
1 * 52000 + 1 * 37000 + 1 * 29000, SDS-PAGE
additional information
-
composed of more than 10 different protein subunits
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
X-ray data: subunits form a dimeric quarternary structure that may also exist under physiological conditiones
additional information
-
subunit arrangement
additional information
-
13 different subunits in 1/1 stoichoimetric amounts
additional information
-
differences in small subunit composition depending on source of enzyme
additional information
-
definitions of functional unit
additional information
-
subunit analysis by reverse phase HPLC
additional information
-
subunit structure, arrangement of subunits in enzyme complex
additional information
-
amino acid sequence of subunit IV
additional information
-
separation of subunits
additional information
-
role of subunit III in the mechanism of the proton pump
additional information
-
sequence alignments of subunits I, II and III of various eukaryotic and prokaryotic organisms
additional information
-
hydrophilic domains of COX subunit III are conformationally linked to the electron transfer function of the enzyme in subunit I and II. Subunit III may serve as a regulatory subunit for COX electron transfer and proton pumping activities
additional information
dilution of the purified protein causes dissociation of the dimer to the monomer. When the pH is raised to 7.4 or 8.5, the protein also shifts from the dimer to the monomer. In solution, CcO is in an equilibrium state between the dimer and monomer
additional information
-
dilution of the purified protein causes dissociation of the dimer to the monomer. When the pH is raised to 7.4 or 8.5, the protein also shifts from the dimer to the monomer. In solution, CcO is in an equilibrium state between the dimer and monomer
additional information
-
enzyme complex lacking subunit III exhibits a shorter catalytic life span and absence of subunit III dramatically slows proton uptake to the active site via the D proton pathway. Arachidonic acid stimulates proton uptake by the D pathway and retards suicide inactivation. Average catalytic life span of detergent-solubilized complex lacking subunit III decreases dramatically with pH. Maintenance of rapid proton transfer through the D pathway and the backflow/exit pathway is one mechanism by which subunit III normally functions to prevent uicide inactivation of cytochrome c oxidase
additional information
-
13 different subunits in 1/1 stoichoimetric amounts
additional information
-
approx. 10 different subunits after 2D gel electrophoresis
additional information
-
enzyme complex of 7 polypeptide components
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
mitochondrial cytochrome oxidase c tends to be a dimer
additional information
-
it is suggested that the mitochondrial encoded subunits I, II and III are the catalytic core of the enzyme
additional information
-
13 different subunits in 1/1 stoichoimetric amounts
additional information
-
-
additional information
-
13 different subunits in 1/1 stoichoimetric amounts
additional information
-
copper-binding protein SCO1 is involved in the assembly of mitochondrial cytochrome-c oxidase. It functions not as a cytochrome-c oxidase copper chaperone, but rather as a mitochondrial redox signaling molecule
additional information
-
enzyme interacts with hepatitis B virus X protein
additional information
-
-
additional information
-
-
additional information
-
proposed folding patterns of subunits
additional information
-
proposed folding patterns of subunits
additional information
-
enzyme complex of 13 polypeptide components
additional information
-
13 different subunits in 1/1 stoichoimetric amounts
additional information
-
brain enzyme from swayback-diseased animals is deficient of subunits II, III and IV
additional information
-
-
additional information
-
liver enzyme, 1/1 stoichiometry of subunits
additional information
-
13 different subunits in 1/1 stoichoimetric amounts
additional information
-
fetal enzyme complex differs from adult heart complex by migration differences of subunits VIa and VIII
additional information
-
the enzyme is built up with both nucleus and mitochondrion-encoded subunits
additional information
-
upon exposure of cells to hypoxia, enzyme subunit IV interacts with protein kinase Cepsilon resulting in increase in cytochrome c oxidase activity
additional information
-
-
additional information
-
proposed folding patterns of subunits
additional information
-
enzyme complex contains eleven rather than twelve subunits
additional information
-
overview nomenclature systems
additional information
-
overview nomenclature systems
additional information
-
sequence alignment with bovine heart
additional information
-
enzyme complex of 9 polypeptide components
additional information
-
13 different subunits in 1/1 stoichoimetric amounts
additional information
-
subunits I, II, and III detected by immunoblotting, a mitochondria-like subunit IV that may confer allosteric properties to the enzyme is also suggested
additional information
-
subunits I, II, and III detected by immunoblotting, a mitochondria-like subunit IV that may confer allosteric properties to the enzyme is also suggested
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A205T
-
mutation in subunit III associated with mitochondrial disease, no change in subunit composition of the complex
D132A
-
mutation of initial proton acceptor of the D pathway. Average catalytic life span of D132A complex lacking subunit III is 2-fold to 50-fold less than that of wild-type complex lacking subunit III, depending upon pH, and the catalytic life span of D132A complex lacking subunit III is independent of external pH from pH 6.2 to pH 7.4
D132A/R481K
-
catalytic life span of D132A/R481K holo complex is 10fold shorter than that of wild-type holo complex
D132N
-
proton donor E286 is present, but its reprotonation from the N side of the membrane is blocked
D151Q/E152N
-
similar steady-state kinetic as wild-type
D188Q/E189N
-
similar steady-state kinetic as wild-type
D195N
-
decrease in activity, increase in Km
D214N
-
decrease in activity, increase in Km
D407A
-
similar properties as wild type, suggesting that D407 does not play a role in proton translocating
D407C
-
similar properties as wild type, suggesting that D407 does not play a role in proton translocating
D407N
-
similar properties as wild type, suggesting that D407 does not play a role in proton translocating
D485A
-
mutant enzyme is active, binds to Ca2+ reversibly, and exhibits the red shift in the heme a absorption spectrum upon Ca2+ binding for both reduced and oxidized states of heme a. Sodium ions reverse the Ca2+-induced red shift of heme a and dramatically decrease the rate of Ca2+ binding to the mutant enzyme. With the mutant enzyme, 1 Ca2+ competes with 1 Na+ for the binding site
E101A/H96A
-
exhibits low activity and eliminates metal binding at this site. Significant activity is restored by adding lipophilic carboxylic compounds (arachidonic acid and cholic acid), but not by their non-carboxylic analogues. Activity is still inhibited by zinc, but this remaining inhibition is nearly eliminated by removal of subunit III
E101C
-
mutation in subunit II strongly reduces oxidase activity to 8%
E101D
-
mutation in subunit II strongly reduces oxidase activity to 16%
E101H
-
mutation in subunit II strongly reduces oxidase activity to 19%
E101I
-
mutation in subunit II strongly reduces oxidase activity to 8%
E101N
-
mutation in subunit II strongly reduces oxidase activity to 17%
E101Q
-
mutation in subunit II strongly reduces oxidase activity to 14%
E10A
the mutant shows 50% of wild type activity
E148Q
-
decrease in activity, increase in Km
E157Q
-
decrease in activity, increase in Km
E286A/I112E
-
about 2% of wild-type activity in the holo complex, mutant complex lacking subunit III exhibits a very short average catalytic life span of approximately 100 catalytic cycles
E286D
-
mutation in D pathway. E286D complex lacking subunit III exhibits a 75% decrease in its O2 reduction activity, compared to wild-type complex lacking subunit III. Catalytic life span of detergent-solubilized E286D complex lacking subunit III is half that of wild-type complex lacking subunit III or about the same as D132A complex lacking subunit III
E286Q
-
absence of both protonic phases in enzyme kinetics. Mutant is not able to generate the ferryl-oxo form under the experimental conditions applied
E54A/D485A
-
inactive mutant enzyme does not assemble normally
E54L
-
inactive mutant enzyme does not assemble normally
E54L/D485A/Q61L
-
inactive mutant enzyme does not assemble normally
E54L/Q61L
-
inactive mutant enzyme does not assemble normally
F86A
-
mutation in subunit III, results in an enzyme complex that contains only about 50-70% of subunit III compared with wild-type
F93A
-
mutation in subunit III, results in an enzyme complex that contains only about 40-60% of subunit III compared with wild-type
G78S
-
mutation in subunit III associated with mitochondrial disease, no change in subunit composition of the complex
H260N
-
mutant of CuA center, the rate constant for the intramolecular electron transfer from heme c to CuA is decreased from 40000 per s for the wild-type enzyme to 11000 for the mutant enzyme, the rate constant for intracomplex electron transfer from CuA to heme a is decreased from 90000 per s for wild-type enzyme to 45 per s for the mutant. The rate constant for the reverse reaction, heme A to CuA, is 180 per s for the mutant enzyme, compared to 17000 for the wild-type enzyme. The redox potential of CuA is increased by 90 mV relative to hemeA
H300A
-
mutation in subunit I increases oxidase activity to 111%
L100AV
-
mutation in subunit II increases oxidase turnover to 45%
L145A/L196A/L203A
-
mutation in subunit I at sites in contact with the fatty acid tails of subunit III, no effect on the content of subunit III in the complex
M263L
-
mutant of CuA center, the rate constant for the intramolecular electron transfer from heme c to CuA is decreased from 40000 per s for the wild-type enzyme to 16000 for the mutant enzyme, the rate constant for intracomplex electron transfer from CuA to heme a is decreased from 90000 per s for wild-type enzyme to 4000 per s for the mutant. The rate constant for the reverse reaction, hemeA to CuA, is 66000 per s for the mutant enzyme, compared to 17000 for the wild-type enzyme. The redox potential of CuA is increased by 120 mV relative to hemeA
M55A
-
mutation in subunit III, results in an enzyme complex that contains only about 30-50% of subunit III compared with wild-type
N139C
in this mutants, proton back leakage through the D-channel is kinetically favored over proton pumping due to the loss of a kinetic gate in the N139 region
N139D
-
turnover rate is increased by a factor of 2-3, mutant does not pump protons
N139L
in this mutant, the bulky L139 side chain inhibits timely reprotonation of E286 through the D-channel, which impairs both proton pumping and the chemical reaction
N139T
in this mutants, proton back leakage through the D-channel is kinetically favored over proton pumping due to the loss of a kinetic gate in the N139 region
Q61A
-
mutant enzyme is active and retains tighly bound Ca2+
Q61L
-
mutant enzyme is active and retains tighly bound Ca2+
R137A
-
mutation in subunit I, results in an enzyme complex that contains only about 5-25% of subunit III compared with wild-type
R226A
-
mutation in subunit III, results in an enzyme complex that contains only about 90% of subunit III compared with wild-type
R481K
-
mutant retains substantial activity and is able to pump protons, but at somewhat reduced rates and stoichiometry
R482A
-
mutant retains substantial activity and is able to pump protons, but at somewhat reduced rates and stoichiometry
R482K
-
mutant retains substantial activity and is able to pump protons, but at somewhat reduced rates and stoichiometry
R482P
-
mutant enzyme is perturbed in its structure and is altered in the redox potential difference between heme a and CuA: 18 mV for R482P compared to +46 mV for the wild-type (hemea - CuA). The electron tranport rate between CuA and heme A is also altered from 93000 per s in the wild-type to 50 per s in the oxidized R482P mutant
R482Q
-
mutant retains substantial activity and is able to pump protons, but at somewhat reduced rates and stoichiometry
S200V/S201V
in the double mutant, the proton affinity of E286 is increased, which slows down both proton pumping and the chemical catalysis
S299A
-
mutation in subunit I reduces oxidase activity to 45%
S299E
-
partly active mutant
S89A
-
mutation in subunit III, loss of side-chain interaction between S89 and F86 does not affect assembly of the enzyme complex
T359A
-
mutation of K pathway. Steady-state activity of T359A complex lacking subunit III is 20% that of wild-type complex lacking subunit III, and life span is similar to wild-type
W104V
-
mutation in subunit II reduces oxidase activity to 45%
W105A
-
mutation in subunit II reduces oxidase activity to 50%
W143A
-
similar copper/Fe ratios as wild-type
W143F
-
similar copper/Fe ratios as wild-type
W58A
-
mutation in subunit III, results in an enzyme complex that contains only about 50-70% of subunit III compared with wild-type
W59A
-
mutation in subunit III, results in an enzyme complex that contains only about 50-70% of subunit III compared with wild-type
W59A/F86A
-
mutation in subunit III, results in an enzyme complex that contains only about 60-80% of subunit III compared with wild-type
Y311F
no enzymic activity, protein complex is correctly assembled
E10A
-
the mutant shows 50% of wild type activity
-
D49N
-
the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
D99N
-
the mutant shows strongly increased Km and reduced kcat values compared to the wild type enzyme
E116Q
-
the mutant shows slightly reduced Km and strongly reduced kcat values compared to the wild type enzyme
E139Q
-
the mutant shows increased Km and slightly increased kcat values compared to the wild type enzyme
E64Q
-
the mutant shows increased Km and kcat values compared to the wild type enzyme
E66Q
-
the mutant shows increased Km and kcat values compared to the wild type enzyme
E68Q
-
the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
E84Q
-
the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
E116Q
-
the mutant shows slightly reduced Km and strongly reduced kcat values compared to the wild type enzyme
-
E139Q
-
the mutant shows increased Km and slightly increased kcat values compared to the wild type enzyme
-
E64Q
-
the mutant shows increased Km and kcat values compared to the wild type enzyme
-
E66Q
-
the mutant shows increased Km and kcat values compared to the wild type enzyme
-
E84Q
-
the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
-
A122T
recurrent missense mutation in mitochondrially encoded cytochrome oxidase I found in a variety of human cancer cells
G6930A
-
nonsense mutation in the mitochondrially encoded complex IV subunit 1 gene, which causes a disruption in the assembly and defective activity of complex VI
D124N
-
subunit I mutant. Reduction of heme a3-CuB is severely impaired, about 0.8 H+ is promptly bound synchronously with the reduction of heme a, followed by a much slower protonation associated with the retarded reduction of the heme a3-CuB site
I347Q
-
16% activity compared to the wild type enzyme
K354M
-
subunit I mutant. Reduction of heme a3 is totally impaired, overall H+ uptake within 10 s is significantly smaller than in the wild-type
R473Q
-
16% activity compared to the wild type enzyme
R474Q
-
41% activity compared to the wild type enzyme
R54M
-
low turnover number, changes in spectral properties of heme a, lowered midpoint redox potential, electron transfer from CuA to heme a is impaired
T50A
-
90% activity compared to the wild type enzyme
T50N
-
50% activity compared to the wild type enzyme
V279I
-
50% activity compared to the wild type enzyme
Y280H
-
catalytic site retains its active configuration that allows O2 binding to heme a3
Y339F
-
64% activity compared to the wild type enzyme
Y406F
-
40% activity compared to the wild type enzyme
DELTAW121
-
mutant of the soluble CuA domain, both the coordination structure of the CuA center and the secondary structure of the protein are changed significantly, the electron transfer activity with cytochrome c is inhibited severely
W121L
-
mutant of the soluble CuA domain, both the coordination structure of the CuA center and the secondary structure of the protein are changed significantly, the electron transfer activity with cytochrome c is inhibited severely
W121Y
-
mutant of the soluble CuA domain, stability decreases compared with the wild-type enzyme. The mutant keeps the same secondary structure as the wild-type protein, but can only transfer electrons with cytochrome c at a rate of one-seventh-fold
C30A
-
is growth-compromised on glycerol/lactate. Is compromised in Cu(I) binding
C30A/C62A
-
is growth-compromised. Is more severely compromised than the single C30A mutant. Fails to accumulate in mitochondria. Is compromised in Cu(I) binding
C40A/C52A
-
is functional
H26A
-
is able to propagate on glycerol/lactate medium
H26A/C30A
-
is growth-compromised. Fails to accumulate in mitochondria. Is compromised in Cu(I) binding
R63T
-
is nonfunctional even when expressed as an IM-tethered Cox19 fusion
C30A
-
is growth-compromised on glycerol/lactate. Is compromised in Cu(I) binding
-
C30A/C62A
-
is growth-compromised. Is more severely compromised than the single C30A mutant. Fails to accumulate in mitochondria. Is compromised in Cu(I) binding
-
C40A/C52A
-
is functional
-
H26A
-
is able to propagate on glycerol/lactate medium
-
E101A
-
mutation in subunit II strongly reduces oxidase activity to 8%
E101A
-
exhibits low activity and eliminates metal binding at this site. Significant activity is restored by adding lipophilic carboxylic compounds (arachidonic acid and cholic acid), but not by their non-carboxylic analogues
K362M
-
inactive
K362M
-
enzyme with mutation in subunit I is inactive
additional information
-
mutant lacking Surf1p involved in assembly of cytochrome-c oxidase shows three subpopulations of enzyme with structurally distinct heme a3-CuB active sites, 50% of enzyme lacks heme a3, 10-15% contains heme a3 but lacks CuB. CuA assembly is unaffected
additional information
-
an assembled complex IV is required to maintain the stability of complex I in a mouse cell line with suppressed expression of subunit 4 of complex IV
additional information
-
CcO activity in cox19DLETA cells is less than 10% of wild-type levels
additional information
-
a strain lacking the Cox10 protein responsible for heme A synthesis, results in no expression of functional CytcO
additional information
-
CcO activity in cox19DLETA cells is less than 10% of wild-type levels
-
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analysis
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cytochrome c oxidase modified electrodes can be used to distinguish amino acid sequence variations in proteins such as cytochrome c. This has potential relevance as a diagnostic for disease states, characterization of electron transfer reactions of cytochrome c isolated from ischemic and control hearts
nutrition
-
in beef muscles psoas major, longissimus lumborum, superficial semimembranosus, deep semimembranosus, and semitendinosus, comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity. Colour stability among muscles is variable and metmyoglobin-reducing activity is more useful than total reducing activity for explaining the role of reducing activity in muscle-colour stability
drug development
-
possibility of nonspecific peroxidation of various substances catalyzed by cytochrome oxidase via the peroxidase mechanism, which may contribute to intracellular metabolism of biologically active drugs (under conditions of cardiotoxicity) and other compounds
drug development
-
tumor necrosis factor alpha-mediated CcO inhibition leads to tissue dysoxia, which suppresses aerobic ATP production and causes a shift to the glycolytic pathway. Kinases and phosphatases involved in reversible tumor necrosis factor alpha-mediated CcO phosphorylation may be promising targets for drug development because they act on an end point of cell signaling
drug development
-
tumor necrosis factor alpha-mediated CcO inhibition leads to tissue dysoxia, which suppresses aerobic ATP production and causes a shift to the glycolytic pathway. Kinases and phosphatases involved in reversible tumor necrosis factor alpha-mediated CcO phosphorylation may be promising targets for drug development because they act on an end point of cell signaling
drug development
-
tumor necrosis factor alpha-mediated CcO inhibition leads to tissue dysoxia, which suppresses aerobic ATP production and causes a shift to the glycolytic pathway. Kinases and phosphatases involved in reversible tumor necrosis factor alpha-mediated CcO phosphorylation may be promising targets for drug development because they act on an end point of cell signaling
-
medicine
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at therapeutic concentrations used for asthma relief, theophylline causes inhibition of the lung enzyme and decreases cellular ATP levels, suggesting a mechanism for its clinical action
medicine
A122T, i.e. m.6267G>A is a recurrent missense mutation in mitochondrially encoded cytochrome oxidase I specifically associated with cancer
medicine
-
amyloid beta which is involved in Alzheimers disease, specifically inhibits cytochrome-c oxidase
medicine
-
enzyme isoform cytochrome oxifdase III interacts with hepatitis B virus X protein
medicine
-
in skeletal muscle and brain of patients with mutations in genes SCO2 or SURF1, cytochrome-c oxidase holoenzyme is reduced to 10-20%, and to 10-30% in heart, whereas liver contains normal levels of enzyme. Heart, brain, and skeletal muscle of patients contain accumulated levels of enzyme subcomplexes of different subunits, but lacking subunit COX2. SCO2 is presumably involved in formation of the CuA centre of the COX2 subunit, and the lack of the CuA centre may result in decreased stability of COX2
medicine
-
6W/Kg GSM 900MHz microwaves may affect brain metabolism and neuronal activity (cytochrome c oxidase activity) in rats
medicine
-
a single injection of exogenous cytochrome c 24 h post-cecal ligation and puncture repletes mitochondrial substrate levels for up to 72 h, restores myocardial COX activity, and significantly improves survival
medicine
-
antipsychotic drugs do not alter COX
medicine
-
CO histochemistry, which reflects neuronal activity, is altered at all levels of the auditory system in Relnrl-Orl mutants (with Orleans mutation, which selectively affects cell migration, cell orientation, and to a more limited extent, cell number in the brain tissue)
medicine
-
COX deficiency is a common cause of human mitochondrial disease
medicine
-
cytochrome oxidase deficiency is a result of heme deficiency that may be relevant to the demyelinating phenotype of the neurodegenerative disease Friedreich's ataxia. Heme-based stimulation of ironsulfur cluster biogenesis is a rational strategy for the neurodegenerative disease Friedreich's ataxia
medicine
-
cytochrome oxidase is a metabolic target of caffeine. Stimulation of Cox activity by caffeine via blockade of A2AR signaling may be an important mechanism underlying the therapeutic benefits of caffeine in Parkinsons disease
medicine
cytochrome oxidase is a metabolic target of caffeine. Stimulation of Cox activity by caffeine via blockade of A2AR signaling may be an important mechanism underlying the therapeutic benefits of caffeine in Parkinsons disease
medicine
-
evidence of secondary loss of electron transport chain function (loss of complex II-III activity) resulting from a primary electron transport chain deficiency (of complex IV), which provides a possible mechanism for the progressive nature of mitochondrial encephalomyopathies and why in some patients multiple patterns of electron transport chain deficiencies may be demonstrated
medicine
-
hypoxia synergises with NO from neuronal nitric oxide synthase to induce neuronal death via cytochrome oxidase inhibition causing neuronal depolarisation. Neuronal nitric oxide synthase activity sensitises the cells to hypoxic-inhibition of cytochrome oxidase
medicine
-
in HIV-associated dementia, cortical neurons demonstrate decreased respiration upon HIV-1 neurotoxin trans activator of transcription proteint treatment, consistent with inhibition of the enzyme
medicine
-
lack of energy after traumatic brain injury caused by inhibition of CcO may be an important aspect of trauma pathology
medicine
-
low prenatal Cu intake by dams is the determinant of CCO activity in cardiac mitochondria of 21-d-old offspring and may lead to the assembly of a less-than-fully active holoenzyme
medicine
-
myocardial CcOX impairment can underlie CO induced cardiac dysfunction
medicine
-
protein kinase C epsilon is activated by hypoxia, which results in the activation of the mitochondrial protein CytCOx, which can protect the lens from mitochondrial damage under naturally hypoxic conditions observed in this tissue
medicine
-
recovery of enhanced cytochrome-c oxidase activity may play a role in ischemic preconditioning protection
medicine
-
relationship between the allosteric ATP-inhibition and phosphorylation of CcO subunit I, which apparently occurs in living cells, but is lost under stress (e.g. hypoxic stress)
medicine
-
relationship between the allosteric ATP-inhibition and phosphorylation of CcO subunit I, which apparently occurs in living cells, but is lost under stress (e.g. hypoxic stress)
medicine
-
simultaneous decrease in 2-deoxyglucose uptake and increase in COI mRNA expression are difficult to reconcile with the current model of basal ganglia function and suggest that the mechanisms by which high-frequency stimulation of the subthalamic nucleus exerts its clinical benefits are more complex than a simple reversal of abnormal activity in the subthalamic nucleus and its targets
medicine
-
the cholinesterase and monoamine oxidase inhibitor ladostigil may have a beneficial effect on cognitive deficits in Alzheimer's disease patients that have a reduction in cortical COx activity and cholinergic hypofunction
medicine
-
mutations in various mitochondrial enzymes can result in Leigh syndrome, among them cytochrome c oxidase
medicine
-
the copper-enzyme cytochrome c oxidase has been indicated as a primary molecular target of mutant copper, zinc superoxide dismutase in familial amyotrophic lateral sclerosis
medicine
-
cytochrome oxidase is a metabolic target of caffeine. Stimulation of Cox activity by caffeine via blockade of A2AR signaling may be an important mechanism underlying the therapeutic benefits of caffeine in Parkinsons disease
-
additional information
100% homology among cox1 sequences from morphotype 1 (females presenting caudal tips smooth without spines) and morphotype 2 (females presenting caudal tips smooth with spines) of Filaria martis collected from beech martens, thus indicating that the shape of female posterior edge may vary among specimens
additional information
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100% homology among cox1 sequences from morphotype 1 (females presenting caudal tips smooth without spines) and morphotype 2 (females presenting caudal tips smooth with spines) of Filaria martis collected from beech martens, thus indicating that the shape of female posterior edge may vary among specimens
additional information
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an assembled complex IV helps to maintain complex I (NADH-ubiquinone oxidoreductase) in mammalian cells
additional information
-
an assembled complex IV helps to maintain complex I (NADH-ubiquinone oxidoreductase) in mammalian cells
additional information
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Arabidopsis thaliana COX19 genes encode functional homologues of the yeast metal chaperone. Smaller COX19-1 isoform, but not the larger one, is able to restore growth on non-fermentable carbon sources when expressed in a yeast cox19 null mutant. Induction by biotic and abiotic stress factors may indicate a relevant role of this protein in the biogenesis of cytochrome c oxidase to replace damaged forms of the enzyme. COX19 has additional functions besides its participation in COX assembly as, for example, metal transport, detoxification, or general protection against oxidative stress
additional information
-
counteracting relationship exists between the effects of withdrawal and 17beta-estradiol on the activity of COX in a subunit specific manner, which may not alter protein synthesis
additional information
-
cytochrome c oxidase is involved in mercury reduction in Acidithiobacillus ferrooxidans cells. Levels of mercury resistance in Acidithiobacillus ferrooxidans strains correspond well with the levels of mercury resistance of cytochrome c oxidase
additional information
-
inhibition of COX activity is rather caused by ischemia-induced modification of COX polypeptides than by inhibition of mitochondrial translation
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, variation within Amiota spp. is 21.8%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, variation within Amiota spp. is 21.8%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, variation within Amiota spp. is 21.8%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, with a variation within Phortica spp. of 1.6%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, with a variation within Phortica spp. of 1.6%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, with a variation within Phortica spp. of 1.6%
additional information
-
molecular phylogenic analysis based on COXI indicates Gobiocypris rarus belongs to Gobioninae. Comparison of DNA with cDNA shows that RNA editing phenomenon does not occur in the COXI of Gobiocypris rarus
additional information
-
permeabilization of the outer mitochondrial membrane during apoptosis functions not just to release cytochrome c but also to maintain it oxidized via cytochrome oxidase, thus maximizing caspase activation
additional information
-
prion protein may not be involved in regulation of cytochrome c oxidase
additional information
-
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
simple and rapid isolation of COX by immunocapture
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
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the monomeric form of Rhodobacter sphaeroides COX when reconstituted into a phospholipid bilayer is completely functionally active in its ability to perform electron transfer and proton pumping activities of the enzyme