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Information on EC 7.1.1.9 - cytochrome-c oxidase

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EC Tree
IUBMB Comments
An oligomeric membrane heme-Cu:O2 reductase-type enzyme that terminates the respiratory chains of aerobic and facultative aerobic organisms. The reduction of O2 to water is accompanied by the extrusion of four protons. The cytochrome-aa3 enzymes of mitochondria and many bacterial species are the most abundant group, but other variations, such as the bacterial cytochrome-cbb3 enzymes, also exist. All of the variants have a conserved catalytic core subunit (subunit I) that contains a low-spin heme (of a- or b-type), a binuclear metal centre composed of a high-spin heme iron (of a-, o-, or b-type heme, referred to as a3, o3 or b3 heme), and a Cu atom (CuB). Besides subunit I, the enzyme usually has at least two other core subunits: subunit II is the primary electron acceptor; subunit III usually does not contain any cofactors, but in the case of cbb3-type enzymes it is a diheme c-type cytochrome. While most bacterial enzymes consist of only 3--4 subunits, the mitochondrial enzyme is much more complex and contains 14 subunits.
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This record set is specific for:
UNIPROT: P07471
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
cytochrome c oxidase, cytochrome oxidase, complex iv, cytochrome c oxidase subunit i, cytochrome c oxidase subunit 1, cytochrome aa3, cytochrome-c oxidase, coxii, cytochrome a3, cox ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
COX VIa-H
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cytochrome c oxidase
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complex IV (mitochondrial electron transport)
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COXVIAH
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cytochrome a3
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cytochrome aa3
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cytochrome ba3
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cytochrome bb3
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-
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cytochrome c oxidase
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-
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Cytochrome caa3
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cytochrome cbb3
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ferrocytochrome c oxidase
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indophenol oxidase
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indophenolase
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oxidase, cytochrome
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Warburg's respiratory enzyme
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ferrocytochrome-c:oxygen oxidoreductase
An oligomeric membrane heme-Cu:O2 reductase-type enzyme that terminates the respiratory chains of aerobic and facultative aerobic organisms. The reduction of O2 to water is accompanied by the extrusion of four protons. The cytochrome-aa3 enzymes of mitochondria and many bacterial species are the most abundant group, but other variations, such as the bacterial cytochrome-cbb3 enzymes, also exist. All of the variants have a conserved catalytic core subunit (subunit I) that contains a low-spin heme (of a- or b-type), a binuclear metal centre composed of a high-spin heme iron (of a-, o-, or b-type heme, referred to as a3, o3 or b3 heme), and a Cu atom (CuB). Besides subunit I, the enzyme usually has at least two other core subunits: subunit II is the primary electron acceptor; subunit III usually does not contain any cofactors, but in the case of cbb3-type enzymes it is a diheme c-type cytochrome. While most bacterial enzymes consist of only 3--4 subunits, the mitochondrial enzyme is much more complex and contains 14 subunits.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-16-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
show the reaction diagram
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-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CX6A2_BOVIN
97
0
10800
Swiss-Prot
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murray, J.; Schilling, B.; Row, R.H.; Yoo, C.B.; Gibson, B.W.; Marusich, M.F.; Capaldi, R.A.
Small-scale immunopurification of cytochrome c oxidase for a high-throughput multiplexing analysis of enzyme activity and amount
Biotechnol. Appl. Biochem.
48
167-178
2007
Bos taurus, Bos taurus (P00396), Bos taurus (P00415), Bos taurus (P00423), Bos taurus (P00426), Bos taurus (P00428), Bos taurus (P00429), Bos taurus (P00430), Bos taurus (P04038), Bos taurus (P07470), Bos taurus (P07471), Bos taurus (P10175), Bos taurus (P13183), Bos taurus (P13184), Homo sapiens
Manually annotated by BRENDA team