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Enzyme Nomenclature
Information on EC 1.9.3.1 - cytochrome-c oxidase
for references in articles please use BRENDA:EC1.9.3.1
Word Map on EC 1.9.3.1
- 1.9.3.1
-
hazard
-
kaplan-meier
- women
- carcinoma
- cardiovascular
-
univariate
- diabetes
-
national
-
all-cause
-
enrol
-
covariates
-
resect
-
population-based
-
5-year
-
registry
-
comorbidities
- artery
-
confound
-
demographic
- stroke
- node
-
december
-
gender
- renal
-
january
- cardiac
- myocardial
-
worse
-
smoking
-
log-rank
-
lymph
- metastasis
- coronary
- infarction
-
stratified
- hypertension
-
clinicopathological
-
admission
-
progression-free
-
stratification
-
postoperative
-
ejection
-
staging
-
preoperative
-
disease-free
-
radiotherapy
-
cyclooxygenase
- medicine
- nutrition
- analysis
- drug development
-
revascularization
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.9.3.1
-
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RECOMMENDED NAME
GeneOntology No.
cytochrome-c oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of O2 reduction; mechanism of proton pumping; proposal for complete turnover cycle, i.e. intramolecular electron transfer, O2 reduction and proton pumping
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of O2 reduction; mechanism of proton pumping; proposal for complete turnover cycle, i.e. intramolecular electron transfer, O2 reduction and proton pumping
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of proton pumping; reaction mechanism
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of proton pumping; reaction mechanism
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of proton pumping
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of proton pumping
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of O2 reduction; schematic diagram of cytochrome c oxidase
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of proton pumping
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of proton pumping
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of O2 reduction
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of O2 reduction
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of O2 reduction; mechanism of proton pumping
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
steady-state kinetics
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
steady-state kinetics
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
study of primary intermediates in the reaction of O2 with the fully reduced enzyme
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
reaction mechanism of cytochrome c with O2
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
proposed electron transfer pathway within the cytochrome c-cytochrome c oxidase complex
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of proton pumping
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
mechanism of proton pumping
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
proposed mechanism of proton translocation
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
spectra of the A, PM, F and O itnermediate state of enzyme catalysis by use of a special cuvette to measure optical changes of millisecond freeze-hyperquench powder samples at temperatures below -23°C. Catalytic cycle of cytochrome c oxidase at low temperature is similar to that at room temperature
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
reduction
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
ferrocytochrome-c:oxygen oxidoreductase
A cytochrome of the a type containing copper. The reduction of O2 to water is accompanied by the extrusion of four protons from the intramitochondrial compartment. Several bacteria appear to contain analogous oxidases.
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CAS REGISTRY NUMBER
COMMENTARY
9001-16-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
recombinant enzyme expressed in Escherichia coli, comparison with human and Arabidosis thaliana enzyme
-
-
individuals with SM and RM mitochondrial genomes are differentiated with the amplification of a 750 bp region of the cox1 gene, accession numbers EU018148 to EU018204; male, standard male, SM, and recently masculinized, RM, types
UniProt
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
recombinant enzyme expressed in Escherichia coli, comparison with human and horse enzyme
-
-
-
395995, 396000, 396001, 396002, 396003, 396004, 396006, 396007, 396009, 396014, 396016, 396019, 396028, 396032, 396033, 396035, 396037, 396038, 396039, 396040, 396041, 396043, 396049, 396050, 396052, 396056, 396058, 396063, 396064, 396065, 396066, 396067, 396078, 396080, 396084, 396092, 396101, 396102, 396104, 396106, 396107, 396108, 396109, 396111, 396118, 396123, 396125, 396126, 396131, 396132, 396133, 657655, 658173, 658620, 659507, 659582, 673702, 674131, 676865, 691023, 691038, 691404, 691758, 693006, 693098, 694175, 711289, 724436, 741541, 742086, 742135, 743264
-
-
-
UniProt
comparison of two oxidized states of enzyme, the state as isolated in the fast form, and the form obtained immediately after oxidation of fully reduced cytochrome-c oxidase with O2. No observable differences are found between these two states
-
-
-
395991, 395992, 395994, 395997, 396000, 396001, 396002, 396005, 396007, 396008, 396012, 396013, 396050, 396057, 396100, 396109, 396110, 700992
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-
-
396002, 396032, 396055, 396065, 674427, 674791, 675018, 675528, 675538, 688882, 690326, 691050, 691404, 692575, 692992, 698934, 724411, 742002, 743020
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-
recombinant enzyme expressed in Escherichia coli, comparison with Arabidopsis thaliana and horse enzyme
-
-
-
658633, 659932, 692264, 692992, 694387, 694987, 695140, 697203, 699003, 699664, 700420, 742002, 742243
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-
-
395028, 395991, 395995, 395996, 396003, 396034, 396042, 396044, 396060, 396134, 396137, 658057, 671947, 672326, 691038, 691335, 693008, 725643, 741886, 741953
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-
-
396000, 396002, 396032, 396035, 396043, 396047, 396065, 396088, 396089, 396117, 396118, 657516, 657776, 658200, 658633, 660014, 671844, 672953, 690359, 692708, 694175, 694263, 694592, 695076, 700077, 711289, 712326, 712814, 713547, 742031, 742816, 743634
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-
-
395028, 395996, 396079, 396120, 396122, 396130, 657924, 657937, 657975, 658073, 672022, 672108, 672326, 672354, 674434, 690895, 691023, 694959, 741933, 742022, 743039
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-
-
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-
all 44 partially or totally sequenced cyanobacterial genomes are analyzed for the occurence of cytM and its putative electron acceptor cytochrome c oxidase
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
a site-specific target disturbance of the electron transport chain at complex IV is a possible source for CH4 formation in plant cells
malfunction
-
a site-specific target disturbance of the electron transport chain at complex IV is a possible source for CH4 formation in plant cells
malfunction
-
a site-specific target disturbance of the electron transport chain at complex IV is a possible source for CH4 formation in plant cells
malfunction
-
T cell cytochrome c oxidase dysfunction results in apoptosis in vitro
malfunction
-
a CcoM deletion strain displays altered growth rates under anaerobic denitrifying conditions
malfunction
-
cardiomyocyte hypertrophy induced by phenylephrine is accompanied by suppression of cytochrome c oxidase activity
malfunction
-
a CcoM deletion strain displays altered growth rates under anaerobic denitrifying conditions
-
metabolism
-
the cytochrome c oxidase plays an important role in regulating endogenous nitric oxide concentrations
metabolism
-
cytochrome c oxidase is the terminal enzyme in the respiratory electron transport chain of mitochondria. It catalyzes the reduction of oxygen to water to generate the electrochemical proton gradient across the mitochondrial membrane that powers the production of ATP. The enzyme takes up four electrons from the positively charged P side (outside) of the membrane and four protons from the negatively charged N side (inside) for the reduction of dioxygen to two water molecules
physiological function
-
the enzyme is a specific intra-mitochondrial site of age-related deterioration, which has a broad impact on mitochondrial physiology. The decline in enzyme activity during aging is associated with selective losses in the levels of both nuclear and mitochondrial DNA-encoded enzyme subunits
physiological function
-
cytochrome c oxidase regulates activation and proliferation in T cells through apoptosis
physiological function
-
COX11 is a mitochondrial chaperone, which plays an important role for plant growth and pollen germination as an essential cytochrome c oxidase complex assembly factor
physiological function
-
cytochrome c oxidase plays a vital role in mitigating given light stress
physiological function
-
CcoM plays a role in anaerobic respiration
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3,5,6-tetramethyl-p-phenylendiamine + O2 + H+
? + H2O
-
-
-
-
-
ascorbate + O2
? + H2O
-
reaction of enzyme in detergent solution and reconstituted in phospholipid vesicles
-
-
?
ferrocytochrome c(H) + O2
ferricytochrome c(H) + H2O
-
-
-
-
?
oxidized horse heart cytochrome c + H2O
reduced horse heart cytochrome c + O2 + H+
-
-
-
-
?
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 + 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 Homo sapiens cytochrome c + O2
oxidized Homo sapiens cytochrome c + H2O
-
relative activity 0.44%
-
-
?
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%
-
-
?
2,3,5,6-tetramethyl-p-phenylenediamine + O2
? + H2O
-
-
-
-
?
4 ferrocytochrome c + O2 + 4 H+
4 ferricytochrome c + 2 H2O
-
-
-
?
4 ferrocytochrome c + O2 + 4 H+
4 ferricytochrome c + 2 H2O
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Q5SJ79;, Q72H23;
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
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
-
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
-
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
-
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
-
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
-
Magnetospirillum magnetotacticum cytochrome c550
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
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
-
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
-
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
-
horse 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
-
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
-
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
-
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
-
Saccharomyces cerevisiae cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome 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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
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
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
Pseudomonas stutzeri ZoBell / ATCC 14405
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + 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 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+