Information on EC 1.9.3.1 - cytochrome-c oxidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.9.3.1
-
RECOMMENDED NAME
GeneOntology No.
cytochrome-c oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aerobic respiration I (cytochrome c)
-
-
aerobic respiration II (cytochrome c) (yeast)
-
-
arsenite oxidation I (respiratory)
-
-
Fe(II) oxidation
-
-
Metabolic pathways
-
-
oxidative phosphorylation
-
-
Oxidative phosphorylation
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-16-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
PCC6301
-
-
Manually annotated by BRENDA team
Anabaena sp. PCC6301
PCC6301
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain W23
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
blacknose shark
-
-
Manually annotated by BRENDA team
dusty shark
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
overview
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-
Manually annotated by BRENDA team
recombinant enzyme expressed in Escherichia coli, comparison with human and Arabidosis thaliana enzyme
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-
Manually annotated by BRENDA team
aerobic photoheterotroph
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-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
tiger shark
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
formerly Bacillus stearothermophilus strain K1041
-
-
Manually annotated by BRENDA team
formerly Bacillus stearothermophilus strain K1041
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
Metapenaeus sp.
-
-
-
Manually annotated by BRENDA team
Mus musculus C57B6/S129
C57B6/S129 mice
SwissProt
Manually annotated by BRENDA team
Mus musculus C57BL/6
C57BL/6 mice
-
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
cultivar BY-2
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-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
Manually annotated by BRENDA team
PCC8009
-
-
Manually annotated by BRENDA team
Nostoc sp. PCC8009
PCC8009
-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
animals suffering from enzootic ataxia i.e. swayback-disease
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-
Manually annotated by BRENDA team
subunit 1-beta and subunit 2
P98002 and P08306
UniProt
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
pea
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain IFO 3445
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-
Manually annotated by BRENDA team
Accession number of subunit 2 of Aa3 oxidase; strain KT2240
UniProt
Manually annotated by BRENDA team
Accession number of subunit 2 of Aa3 oxidase; strain KT2240
UniProt
Manually annotated by BRENDA team
AM1
-
-
Manually annotated by BRENDA team
AM1
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Rattus norvegicus Charles-Foster
adult male albino rats of Charles-Foster strain
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-
Manually annotated by BRENDA team
atlantic sharpnose shark
-
-
Manually annotated by BRENDA team
thermohalophilic bacterium
-
-
Manually annotated by BRENDA team
strain BY4742
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-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
synthetic construct
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-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
var. Titan Red, wheat
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3,5,6-tetramethyl-p-phenylendiamine + O2 + H+
? + H2O
show the reaction diagram
-
-
-
-
-
2,3,5,6-tetramethyl-p-phenylenediamine + O2
? + H2O
show the reaction diagram
3,3'-diaminobenzidene-tetrahydrochloride + O2 + H+
? + H2O
show the reaction diagram
amidopyrine + H2O2
?
show the reaction diagram
-
-
-
-
?
ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
ascorbate + O2
? + H2O
show the reaction diagram
-
reaction of enzyme in detergent solution and reconstituted in phospholipid vesicles
-
-
?
benzidine + H2O2
?
show the reaction diagram
-
-
-
-
?
diaminobenzidine + H2O2
?
show the reaction diagram
-
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
show the reaction diagram
ferrocytochrome c + O2
ferricytochrome c + H2O
show the reaction diagram
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
show the reaction diagram
ferrocytochrome c(H) + O2
ferricytochrome c(H) + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c-550 + O2
ferricytochrome c-550 + H2O
show the reaction diagram
-
-
-
-
?
melatonin + H2O2
?
show the reaction diagram
-
-
-
-
?
N,N,N',N'-tetramethyl-p-phenylenediamine + O2
?
show the reaction diagram
-
-
-
-
?
o-dianisidine + H2O2
?
show the reaction diagram
oxidized horse heart cytochrome c + H2O
reduced horse heart cytochrome c + O2 + H+
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + H2O2
?
show the reaction diagram
-
-
-
-
?
peroxynitrite
NO + O22-
show the reaction diagram
-
enzyme must be fully reduced, proposed reaction
-
?
reduced Aspergillus oryzae cytochrome c + O2
oxidized Aspergillus oryzae cytochrome c + H2O
show the reaction diagram
-
relative activity 2.2%
-
-
?
reduced Bacillus subtilis cytochrome c + O2
oxidized Bacillus subtilis cytochrome c + H2O
show the reaction diagram
-
relative activity 27%
-
-
?
reduced Bos taurus cytochrome c + O2
oxidized Bos taurus cytochrome c + H2O
show the reaction diagram
reduced Bos taurus cytochrome c + O2 + H+
oxidized Bos taurus cytochrome c + H2O
show the reaction diagram
-
-
-
-
?
reduced Bufo vulgaris cytochrome c + O2
oxidized Bufo vulgaris cytochrome c + H2O
show the reaction diagram
-
relative activity 0.73%
-
-
?
reduced Candida krusei cytochrome c + O2
oxidized Candida krusei cytochrome c + H2O
show the reaction diagram
-
relative activity 5.0%
-
-
?
reduced Columba livia cytochrome c + O2
oxidized Columba livia cytochrome c + H2O
show the reaction diagram
-
relative activity 0.44%
-
-
?
reduced cytochrome aa3 + O2 + H+
oxidized cytochrome aa3 + H2O
show the reaction diagram
-
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
show the reaction diagram
reduced cytochrome c551 + O2 + H+
oxidized cytochrome c551 + H2O
show the reaction diagram
reduced Homo sapiens cytochrome c + O2
oxidized Homo sapiens cytochrome c + H2O
show the reaction diagram
-
relative activity 0.44%
-
-
?
reduced horse cytochrome c + O2
oxidized horse cytochrome c + H2O
show the reaction diagram
reduced horse cytochrome c + O2 + H+
oxidized horse cytochrome c + H2O
show the reaction diagram
reduced horse heart cytochrome c + O2 + H+
oxidized horse heart cytochrome c + H2O
show the reaction diagram
reduced Kloeckera sp. cytochrome c + O2
oxidized Kloeckera sp. cytochrome c + H2O
show the reaction diagram
-
relative activity 5.4%
-
-
?
reduced Loligo pealeii cytochrome c + O2
oxidized Loligo pealeii cytochrome c + H2O
show the reaction diagram
-
relative activity 1.2%
-
-
?
reduced Musca domestica cytochrome c + O2
oxidized Musca domestica cytochrome c + H2O
show the reaction diagram
-
relative activity 2.6%
-
-
?
reduced N,N,N',N'-tetramethyl-p-phenylene diamine + O2
oxidized N,N,N',N'-tetramethyl-p-phenylene diamine + H2O
show the reaction diagram
reduced oyster cytochrome c + O2
oxidized oyster cytochrome c + H2O
show the reaction diagram
-
relative activity 0.54%
-
-
?
reduced Physarum polycephalum cytochrome c + O2
oxidized Physarum polycephalum cytochrome c + H2O
show the reaction diagram
-
relative activity 0.9%
-
-
?
reduced Porphyra tenera cytochrome c + O2
oxidized Porphyra tenera cytochrome c + H2O
show the reaction diagram
-
relative activity 15%
-
-
?
reduced prawn cytochrome c + O2
oxidized prawn cytochrome c + H2O
show the reaction diagram
-
relative activity 0.95%
-
-
?
reduced Pseudomonas aeruginosa cytochrome c + O2
oxidized Pseudomonas aeruginosa cytochrome c + H2O
show the reaction diagram
-
relativ activity 100%
-
-
?
reduced Pseudomonas saccharophila cytochrome c + O2
oxidized Pseudomonas saccharophila cytochrome c + H2O
show the reaction diagram
-
relative activity 82%
-
-
?
reduced Rhodospirillum rubrum cytochrome c + O2
oxidized Rhodospirillum rubrum cytochrome c + H2O
show the reaction diagram
-
relative activity 1.7%
-
-
?
reduced Saccharomyces cerevisiae cytochrome c + O2
oxidized Saccharomyces cerevisiae cytochrome c + H2O
show the reaction diagram
-
relative activity 4.9%
-
-
?
reduced salmon cytochrome c + O2
oxidized salmon cytochrome c + H2O
show the reaction diagram
-
relative activity 7.1%
-
-
?
reduced Scombridae gen. sp. cytochrome c + O2
oxidized Scombridae gen. sp. cytochrome c + H2O
show the reaction diagram
-
relative activity 8.7%
-
-
?
reduced shark cytochrome c + O2
oxidized shark cytochrome c + H2O
show the reaction diagram
-
relative activity 1.5%
-
-
?
reduced Styela plicata cytochrome c + O2
oxidized Styela plicata cytochrome c + H2O
show the reaction diagram
-
relative activity 2.2%
-
-
?
reduced Triticum aestivum cytochrome c + O2
oxidized Triticum aestivum cytochrome c + H2O
show the reaction diagram
-
relative activity 1.5%
-
-
?
reduced yeast cytochrome c + O2
oxidized yeast cytochrome c + H2O
show the reaction diagram
tetramethyl-phenylenediamine + O2 + H+
? + H2O
show the reaction diagram
-
-
-
-
?
tetramethylbenzidine + H2O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
show the reaction diagram
ferrocytochrome c + O2
ferricytochrome c + H2O
show the reaction diagram
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
show the reaction diagram
ferrocytochrome c(H) + O2
ferricytochrome c(H) + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Heme a3
heme b
-
non-covalently bound
heme c
protoheme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
contains one Ca2+ per enzyme, tighly bound Ca2+ plays a structural role in the enzyme. Mutant enzyme D485A 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
copper
Iron
-
contains iron
Mg2+
contains Mg2+
Mn
-
when grown with 0.7 mM Mn2+ and 0.05 mM Mg2+, Mn2+ appears to be inserted into what is normally a Mg2+ site
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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 peptide’s 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+
cyanide
Dicyclohexylcarbodiimide
diethylenetriamine-NONOate
-
-
ethylene glycol
-
inhibits by reducing electron flow between cytochrome a and cytochrome a3
ferricytochrome c
-
-
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
nitric oxide
NO2-
-
competitive inhibitor
Nonionic detergents
-
-
-
peroxynitrite
-
0.1 mM, complete inhibition
phosphate
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
potassium cyanide
Salicyl aldoxime
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
-
Sodium azide
Sodium deoxycholate
-
-
Sulfide
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
Triton X-100
Tumor necrosis factor alpha
Tween 20
-
0.5%, 40% inhibition
Tween 80
-
0.5% 60% inhibition
additional information