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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
?
-
-
-
-
?
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
-
-
-
-
?
melatonin + H2O2
?
-
-
-
-
?
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
-
?
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
-
horse ferrocytochrome c
-
-
?
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
-
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
-
Crithidia fasciculata cytochrome 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
-
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
-
-
-
-
?
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
-
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
-
-
-
-
?
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
-
-
-
-
?
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+
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+
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+
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+
ferricytochrome c + H2O
-
-
-
-
?
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-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
-
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 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
?
-
-
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
?
-
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
?
-
-
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
?
-
-
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
-
-
lysophophatidylcholine
-
-
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
-
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
-
0.1 mM, 50% inhibition
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-
-
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-
-
0.0013 mM, 50% 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
-
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
-
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
-
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
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
-
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