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Information on EC 7.1.1.9 - cytochrome-c oxidase
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7.1.1.9 cytochrome-c oxidaseIUBMB 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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Word Map
- 7.1.1.9
-
kaplan-meier
-
univariate
- women
- cardiovascular
-
all-cause
-
january
-
log-rank
-
population-based
-
resect
-
5-year
- metastasis
-
december
-
worse
-
stratified
-
confound
- node
-
registry
- cardiac
-
comorbidities
-
demographic
- coronary
-
smoke
- myocardial
- artery
- hypertension
-
smoking
- infarction
-
postoperative
-
covariates
-
clinicopathological
-
admission
-
endpoint
-
surveillance
-
disease-free
-
preoperative
-
high-risk
-
radiotherapy
-
progression-free
-
stratification
-
insurance
-
eligible
- atrial
-
oncology
-
cyclooxygenase
-
ejection
-
staging
-
interquartile
- nutrition
- medicine
- drug development
- analysis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
4
+
+
4
=
4
+
2
4
+
+
8
=
4
+
2
+
4
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aa3 terminal Oxidase
ba3-type cytochrome c oxidase
caa3-type cytochrome c oxidase
cbb3 cytochrome c oxidase
cbb3-2 oxidase
cbb3-2 terminal oxidase
cbb3-CcO
cbb3-cytochrome c oxidase
cbb3-type cytochrome c oxidase
CCO
CcoM
CcOX
COI
complex IV
complex IV (mitochondrial electron transport)
-
-
-
-
COX
Cox 1
COX I
COX IV
COX Vb
COX1
COX19
COX4
Cox7c
COXI
COXII
COXVIAH
-
-
-
-
CytcO
cytochrome a3
-
-
-
-
cytochrome aa3
cytochrome ba3
-
-
-
-
cytochrome bb3
-
-
-
-
cytochrome bo3 oxidase
cytochrome bo3-type cytochrome c oxidase
cytochrome c oxidase
cytochrome c oxidase subunit 1
Cytochrome caa3
-
-
-
-
cytochrome cbb3
-
-
-
-
cytochrome oxidase
cytochrome oxidase subunit II
cytochrome oxidase VIIc
cytochrome-c oxidase I
cytochrome-c oxidase subunit I
CytOX
EC 1.9.3.1
-
-
formerly
-
ferrocytochrome c oxidase
-
-
-
-
indophenol oxidase
-
-
-
-
indophenolase
-
-
-
-
MCOX2
NADH cytochrome c oxidase
-
-
incorrect
-
oxidase, cytochrome
-
-
-
-
Warburg's respiratory enzyme
-
-
-
-
cytochrome aa3
-
-
-
-
cytochrome c oxidase
-
-
-
-
cytochrome c oxidase
-
-
cytochrome c oxidase
-
cytochrome c oxidase
-
-
cytochrome c oxidase
-
-
cytochrome c oxidase
-
-
cytochrome oxidase
-
-
ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 ferrocytochrome c + O2 + 8 H+[side 1] = 4 ferricytochrome c + 2 H2O + 4 H+[side 2]
-
-
-
-
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
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
-
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
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
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
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
reaction mechanism of cytochrome c with O2
-
4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
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 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 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 electron transfer pathway within the cytochrome c-cytochrome c oxidase complex
-
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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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.
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CAS REGISTRY NUMBER
COMMENTARY
9001-16-5
-
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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-1,4-phenylenediamine + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + H2O
reduced ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine + H2O
-
-
-
-
r
reduced ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + H2O
reduced Aspergillus oryzae cytochrome c + O2
oxidized Aspergillus oryzae cytochrome c + H2O
-
relative activity 2.2%
-
-
?
reduced Bacillus subtilis cytochrome c + O2
oxidized Bacillus subtilis cytochrome c + H2O
-
relative activity 27%
-
-
?
reduced Bos taurus cytochrome c + O2 + 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
-
-
-
?
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
-
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
-
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
-
no proton translocation
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Crithidia fasciculata cytochrome c
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Saccharomyces cerevisiae cytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
flavin semiquinone electron donors lumiflavin, riboflavin or FMN can be used, kinetic analysis
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
horse ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
cytochrome c550 and cytochrome c549
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
Candida krusei ferrocytochrome c
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
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
-
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
-
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
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
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
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
Saccharomyces cerevisiae cytochrome c
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
horse cytochrome c
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
Thermus thermophilus cytochrome c
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
Candida krusei cytochrome c
-
-
r
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
r
ferrocytochrome c550 + O2 + H+
ferricytochrome c550 + H2O
-
-
-
-
r
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
-
-
-
-
r
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
-
-
-
-
r
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
r
O2 + 4 cyt c(Fe2+) + 8 H+/in
2 H2O + 4 cyt c(Fe3+) + 4 H+/out
-
-
-
?
O2 + 4 cyt c(Fe2+) + 8 H+/in
2 H2O + 4 cyt c(Fe3+) + 4 H+/out
-
-
-
?
reduced ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + H2O
-
-
-
-
r
reduced ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + H2O
-
-
-
-
r
reduced ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + H2O
-
-
-
-
?
reduced ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-4-phenylenediamine dihydrochloride + H2O
-
-
-
-
?
reduced Bos taurus cytochrome c + O2
oxidized Bos taurus cytochrome c + H2O
-
-
-
-
?
reduced Bos taurus cytochrome c + O2
oxidized Bos taurus cytochrome c + H2O
-
-
-
-
?
reduced Bos taurus cytochrome c + O2
oxidized Bos taurus cytochrome c + H2O
-
relative activity 0.53%
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
oxidation of cytochrome c by cytochrome oxidase stimulates caspase activation
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
electron exchange of cytochrome c with the electrode with CcO (with a his-tag at the C-terminus of subunit I) immobilized in a protein-tethered bilayer lipid membrane is shown to be mediated by the enzyme if oxygen is present in the bulk solution. The increasing current density in the anodic and cathodic direction in the presence of oxygen may be due to intermediate redox states of the CcO. Hopping mechanism of electron transfer through the enzyme between cytochrome c and the electrode
-
-
?
reduced cytochrome c + O2 + H+
oxidized cytochrome c + H2O
-
-
-
-
?
reduced cytochrome c551 + O2 + H+
oxidized cytochrome c551 + H2O
-
-
-
-
?
reduced cytochrome c551 + O2 + H+
oxidized cytochrome c551 + H2O
-
-
-
-
?
reduced horse cytochrome c + O2
oxidized horse cytochrome c + H2O
-
-
-
-
?
reduced horse cytochrome c + O2
oxidized horse cytochrome c + H2O
-
-
-
-
?
reduced horse cytochrome c + O2 + H+
oxidized horse cytochrome c + H2O
-
-
-
-
?
reduced horse cytochrome c + O2 + H+
oxidized horse cytochrome c + H2O
-
-
-
-
?
reduced horse heart cytochrome c + O2 + H+
oxidized horse heart cytochrome c + H2O
-
-
-
-
?
reduced horse heart cytochrome c + O2 + H+
oxidized horse heart cytochrome c + H2O
-
-
-
-
?
reduced N,N,N',N'-tetramethyl-4-phenylenediamine + O2 + H2
oxidized N,N,N',N'-tetramethyl-4-phenylenediamine + H2O
-
-
-
-
?
reduced N,N,N',N'-tetramethyl-4-phenylenediamine + O2 + H2
oxidized N,N,N',N'-tetramethyl-4-phenylenediamine + H2O
-
-
-
-
?
reduced N,N,N',N'-tetramethyl-p-phenylene diamine + O2
oxidized N,N,N',N'-tetramethyl-p-phenylene diamine + H2O
-
-
-
-
?
reduced N,N,N',N'-tetramethyl-p-phenylene diamine + O2
oxidized N,N,N',N'-tetramethyl-p-phenylene diamine + H2O
-
-
-
-
?
reduced yeast cytochrome c + O2
oxidized yeast cytochrome c + H2O
-
-
-
-
?
reduced yeast cytochrome c + O2
oxidized yeast cytochrome c + H2O
-
-
-
-
?
additional information
?
-
-
accessibility and electrostatic charge of enzyme do not differ in a significant way among human, Arabidopsis thaliana and horse
-
-
?
additional information
?
-
-
numerous organic aromatic compounds, which are not oxidized by cytochrome oxidase via the oxidase mechanism (i.e. using molecular oxygen as the terminal acceptor), can undergo a low rate oxidation by cytochrome oxidase via the peroxidase mechanism. Paracetamol and isonicotinic acid hydrazide are completely resistant to peroxidation by cytochrome oxidase
-
-
?
additional information
?
-
-
cytochrome c oxidase is an efficient energy transducer that reduces oxygen to water and converts the released chemical energy into an electrochemical membrane potential. As a true proton pump, the enzyme translocates protons across the membrane against this potential
-
-
?
additional information
?
-
-
the predominant entry point for protons going into the K-channel of cytochrome oxidase is the surface-exposed glutamic acid E101 in subunit II
-
-
?
additional information
?
-
-
accessibility and electrostatic charge of enzyme do not differ in a significant way among human, Arabidopsis thaliana and horse
-
-
?
additional information
?
-
-
accessibility and electrostatic charge of enzyme do not differ in a significant way among human, Arabidopsis thaliana and horse
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
additional information
?
-
-
the enzyme also shows catalase activity
-
-
?
additional information
?
-
For all mutant strains, the NADH oxidation activity of membranes obtained from aerobic exponentially growing cultures is some higher than that of the wild-type strain (in the range of 1035% higher)
-
-
?
additional information
?
-
-
For all mutant strains, the NADH oxidation activity of membranes obtained from aerobic exponentially growing cultures is some higher than that of the wild-type strain (in the range of 1035% higher)
-
-
?
additional information
?
-
inactivation of the Cbb3-1 terminal oxidase in a strain containing a wild-type ANR gene lead to a 46% decrease in cytochrome b and to a 57% decrease in cytochrome c
-
-
?
additional information
?
-
-
inactivation of the Cbb3-1 terminal oxidase in a strain containing a wild-type ANR gene lead to a 46% decrease in cytochrome b and to a 57% decrease in cytochrome c
-
-
?
additional information
?
-
For all mutant strains, the NADH oxidation activity of membranes obtained from aerobic exponentially growing cultures is some higher than that of the wild-type strain (in the range of 1035% higher)
-
-
?
additional information
?
-
inactivation of the Cbb3-1 terminal oxidase in a strain containing a wild-type ANR gene lead to a 46% decrease in cytochrome b and to a 57% decrease in cytochrome c
-
-
?
additional information
?
-
-
thyroid hormone T3 regulates the expression of COX subunits by both transcriptional and posttranslational mechanism
-
-
?
additional information
?
-
-
cytochrome c purified from mammalian brain is phosphorylated on S47, phosphorylation is lost during ischemia. Both S47-phosphorylated and phosphomimetic cytochrome c show a lower oxygen consumption rate in reaction with isolated Cytc oxidase
-
-
?
additional information
?
-
-
the intermolecular electron transfer kinetics between CytcM and the soluble CuA domain, i.e. the donor binding and electron entry site, of subunit II of cytochrome c oxidase is investigated
-
-
?
additional information
?
-
-
oxygenation of the tetradentate model both in MeCN and in other solvents produces a low-temperature-stable dioxygen-bridged peroxide with an O-O stretching vibration at 799 cm-1. Oxygenation of the tridentate model in EtCN solution generates a heme superoxide species with the copper moiety oxidized to copper(II). Coexistence of a heme superoxide and a bridged peroxide species in equivalent amounts when the oxygenation reaction is carried out in CH2Cl2/7% EtCN
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
ferrocytochrome c(H) + O2
ferricytochrome c(H) + H2O
-
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
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
-
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
-
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
-
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 + 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
Pseudomonas stutzeri ZoBell / ATCC 14405
-
-
-
-
?
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
-
-
-
-
?
additional information
?
-
-
cytochrome c oxidase is an efficient energy transducer that reduces oxygen to water and converts the released chemical energy into an electrochemical membrane potential. As a true proton pump, the enzyme translocates protons across the membrane against this potential
-
-
?
additional information
?
-
-
the predominant entry point for protons going into the K-channel of cytochrome oxidase is the surface-exposed glutamic acid E101 in subunit II
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
additional information
?
-
-
the enzyme also shows catalase activity
-
-
?
additional information
?
-
For all mutant strains, the NADH oxidation activity of membranes obtained from aerobic exponentially growing cultures is some higher than that of the wild-type strain (in the range of 1035% higher)
-
-
?
additional information
?
-
-
For all mutant strains, the NADH oxidation activity of membranes obtained from aerobic exponentially growing cultures is some higher than that of the wild-type strain (in the range of 1035% higher)
-
-
?
additional information
?
-
inactivation of the Cbb3-1 terminal oxidase in a strain containing a wild-type ANR gene lead to a 46% decrease in cytochrome b and to a 57% decrease in cytochrome c
-
-
?
additional information
?
-
-
inactivation of the Cbb3-1 terminal oxidase in a strain containing a wild-type ANR gene lead to a 46% decrease in cytochrome b and to a 57% decrease in cytochrome c
-
-
?
additional information
?
-
For all mutant strains, the NADH oxidation activity of membranes obtained from aerobic exponentially growing cultures is some higher than that of the wild-type strain (in the range of 1035% higher)
-
-
?
additional information
?
-
inactivation of the Cbb3-1 terminal oxidase in a strain containing a wild-type ANR gene lead to a 46% decrease in cytochrome b and to a 57% decrease in cytochrome c
-
-
?
additional information
?
-
-
thyroid hormone T3 regulates the expression of COX subunits by both transcriptional and posttranslational mechanism
-
-
?
additional information
?
-
-
antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
oxidation of heme a+a3 in cytochrome c oxidase of Prnp-/- mice is similar to that in Prnp+/+ mice
heme
-
reduction of dioxygen to water takes place at the heme a3-CuB binuclear center
heme
analysis of the dynamics of the fully reduced (CuA1+ heme b 2+ CuB1+ heme a3 2+) and the mixed valence (CuA2+ heme b 3+ CuB1+ heme a3 2+) forms of the enzyme
heme a
-
CuA and heme a are in electronic equilibrium acting as a redox pair
Heme a3
-
method for quantification of cytochrome c oxidase based upon the distinctive optical signal of the cyanide-ferroheme a3 compound in the visible region
Heme a3
-
Trp-272 is the direct reductant either to the heme a3 oxoferryl species or to CuB2+
heme c
-
2 molecules in minimal structure unit composed of the three subunits
protoheme
-
1 molecule in minimal structure unit composed of the three subunits
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
Cu
Cu2+
Fe
Fe2+
Fe3+
Mg
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
Zn
additional information
copper
-
oxidation of copper in cytochrome c oxidase of Prnp-/- mice is similar to that in Prnp+/+ mice
copper
-
Cox17p specifically binds Cu(I) at a molar copper content of 3.3 under redzuced conditions and significantly activates the mitochondrial. The Cu-Cox17p complex is maintained between pH values from 5.0 to 7.7. Cu is completely released from Cox17p at pH 8.0. The stringent selectivity of Cox17p for cipper is required for enzyme activation
Cu
-
CuB located in subunit I, electron flow from ferrocytochrome c to binuclear center
Cu
-
-
Cu
-
structural interpretations of cytochrome c oxidase metal active sites by X-ray absorption spectroscopy, XAS, studies
Cu
-
-
Cu
-
CuB located in subunit I, electron flow from ferrocytochrome c to binuclear center
Cu
-
0.7 copper atoms in minimal structure unit composed of the three subunits
Cu
-
CuA contains a mononuclear Cu site with 2 cysteine sulfur and 2 imidazole nitrogen atoms as ligands
Cu
-
CuB located in subunit I, electron flow from ferrocytochrome c to binuclear center
Cu
-
recombinant Cox19 binds 1 mol eq of Cu(I) per monomer. Cu(I) binding may be a transient property
Cu
-
reduction of dioxygen to water takes place at the heme a3-CuB binuclear center
Cu2+
-
interaction of inhibitor nitric oxide is either with ferrous heme iron or oxidized copper, but not both simultaneously. The noncompetitive interaction with oxidized copper results in oxidation of NO to nitrite and behaves kinetically as if it has an apparent affinity of 28 nM
Cu2+
-
CuA and heme a are in electronic equilibrium acting as a redox pair. Trp-272 is the direct reductant either to the heme a3 oxoferryl species or to CuB2+
Cu2+
copper-containing enzyme. Contains 4 atoms per molecule of the enzyme
Fe
-
2 Fe per monomeric, catalytic unit of the enzyme, proton-induced X-ray emission study
Fe
-
3.0 iron in minimal structure unit composed of the three subunits
Fe
-
2 Fe per monomeric, catalytic unit of the enzyme, proton-induced X-ray emission study
Fe
-
2 Fe per monomeric, catalytic unit of the enzyme, proton-induced X-ray emission study
Fe2+
-
interaction of inhibitor nitric oxide is either with 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
Zn
-
one-half of Zn is tightly bound to subunit VI, 1 mol per functional unit, X-ray absorption fine structure, EXAFS, studies, Zn may play a structural role
Zn
-
1 Zn per monomeric catalytic unit, proton-induced X-ray emission studies
additional information
-
all redox-active metal centers are contained in subunits I and II
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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 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
Cu2+
-
inhibition of enzyme by amyloid beta depends completely on presence of divalent Cu2+, but not Cu+
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
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
-
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
NaCN
-
1 mM completely inhibits mercury volatilization activities with reduced cytochrome c and 2,3,5,6-tetramethyl-p-phenylendiamine in strain MON-1
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
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, 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
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
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
-
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
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
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
-
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
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
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
Tumor necrosis factor alpha
-
leads to an ca. 60% reduction in CcO activity in hepatocyte homogenates. Shows no direct effect on CcO activity using purified CcO. CcO isolated after tumor necrosis factor alpha treatment shows tyrosine phosphorylation on CcO catalytic subunit I and is ca. 50 and 70% inhibited at high cytochrome c concentrations in the presence of allosteric activator ADP and inhibitor ATP, respectively
-
Tumor necrosis factor alpha
-
leads to reduction in CcO activity in hepatocyte homogenates. Shows no direct effect on CcO activity using isolated mitochondria CcO
-
Zn2+
-
tetrahedral coordination of Zn2+ with two N-histidine imidazoles, one N-histidine imidazol or N-lysine and one O-COOH, possibly located at the entry site ogf the proton conducting D pathway; tetrahedral coordination site(s) for Zn2+ with two N-histidine imidazoles, one N-histidine imidazol or N-lysine and one O-COOH (glutamate or aspartate), possibly located at the entry site of the proton conducting D pathway in the oxidase and involved in inhibition of the oxygen reduction catalysis and proton pumping by internally trapped zinc. Presence of ZnCl2 during liposome reconstitution of cytochrome c oxidase has no effect on the sidedness of the incorporated COX, neither increases the residual amount of soluble COX
Zn2+
-
reaction of enzyme in detergent solution and reconstituted in phospholipid vesicles. At concentrations of Zn2+ below 0.25 mM at the outside of the vesicles, transistion rates between intermediates is not altered. Zn2+ ions bind on both sides of the enzyme and binding at the proton output side selectively impairs proton release during the transition of peroxy intermediate to oxo-ferryl intermediate
Zn2+
-
the Glu-101/His-96 site of subunit II as the site of metal binding inhibits the uptake of protons into the K pathway. Subunit III contributes to zinc binding and/or inhibition of the D pathway
additional information
-
import of COX19 is not inhibited by the ionophore valinomycin indicating that an electrical membrane potential is not required
-
additional information
-
cAMP-dependent tyrosine phosphorylation of subunit I inhibits cytochrome c oxidase activity
-
additional information
-
incubation of the isolated enzyme with protein kinase A, cAMP, and ATP results in serine and threonine phosphorylation of CcO subunit I, which is correlated with sigmoidal inhibition kinetics in the presence of ATP
-
additional information
-
not inhibited by Triton X-100 up to a concentration of 2%
-
additional information
ursodeoxycholateand glycochenodeoxycholate have no observable effect on enzyme activity
-
additional information
-
ursodeoxycholateand glycochenodeoxycholate have no observable effect on enzyme activity
-
additional information
-
high percentage levels of mutated mitochondrial DNA are associated with a dramatic reduction in wild-type levels and COX deficiency. For the m.3243ArG mutation, a superabundance of wild-type mitochondrial DNA is found in many muscle-fiber sections with negligible COX activity
-
additional information
-
knocked down frataxin in oligodendroglioma cells using siRNA produces significant defects in the activity of cytochrome oxidase. Exogenous hemin produces a significant rescue of cytochrome oxidase activity
-
additional information
-
is competitively inhibited early in sepsis and progresses, becoming noncompetitive during the late phase. Exogenous cytochrome c can overcome this myocardial CcOX competitive inhibition. Cecal ligation and puncture inhibit CcOX at 48 h in saline-injected mice. However, cytochrome c injection abrogates this inhibition and restores CcOX kinetic activity to sham values at 48 h
-
additional information
Inactivation of the Aa3 oxidase lead to a 50% reduction in N,N,N',N'-tetramethyl-1,4-benzenediamine (TMPD)-dependent oxidase activity (electron donor specific for cytochrome c-dependent oxidases). Lack of the Cbb3-2 oxidase lead to 65% reduction.; In cells growing exponentially under high oxygen tension (100% air saturation), the absence of ANR lead to a 20fold decrease in mRNA levels of the Cbb3-1 oxidase gene, a decrease that is 10-fold lower than that observed in cells growing exponentially in shaken flasks, and 35-fold lower than in cells entering the stationary phase. When cells are grown under limiting oxygen supply (40% air saturation), the absence of ANR lead to a over 500fold decrease in the mRNA levels of the Cbb3-1 oxidase gene; Under aerobic conditions, inactivation of transcriptional activator gene ANR lead to a significant decrease (more than 230fold) of the mRNA corresponding to the Cbb3-1 oxidase, but have little effect on the other analysed terminal oxidases Cbb3-2 and Aa3.
-
additional information
-
Inactivation of the Aa3 oxidase lead to a 50% reduction in N,N,N',N'-tetramethyl-1,4-benzenediamine (TMPD)-dependent oxidase activity (electron donor specific for cytochrome c-dependent oxidases). Lack of the Cbb3-2 oxidase lead to 65% reduction.; In cells growing exponentially under high oxygen tension (100% air saturation), the absence of ANR lead to a 20fold decrease in mRNA levels of the Cbb3-1 oxidase gene, a decrease that is 10-fold lower than that observed in cells growing exponentially in shaken flasks, and 35-fold lower than in cells entering the stationary phase. When cells are grown under limiting oxygen supply (40% air saturation), the absence of ANR lead to a over 500fold decrease in the mRNA levels of the Cbb3-1 oxidase gene; Under aerobic conditions, inactivation of transcriptional activator gene ANR lead to a significant decrease (more than 230fold) of the mRNA corresponding to the Cbb3-1 oxidase, but have little effect on the other analysed terminal oxidases Cbb3-2 and Aa3.
-
additional information
-
after 30 min of ischemia and 120 min of reperfusion, total COI levels decrease in the left ventricular regions at risk by 72%. Subunit Va is also downregulated by 42% following prolonged ischemia-reperfusion in the left ventricular regions at risk. Cardiac ischemic preconditioning administered before ischemia-reperfusion reduces the loss of COI approximately 30% and prevents COVa losses completely. No losses in subunits Vb and VIIa following ischemia-reperfusion alone, but significant losses occur when cardiac ischemic preconditioning is administered before prolonged ischemia-reperfusion. Delivery of a cell-permeable PKC-epsilon translocation inhibitor to isolated rat hearts before prolonged ischemia-reperfusion dramatically increases COI loss
-
additional information
-
CCO activity, the content of the mitochondrial-encoded CCO subunit 1 (COX1), and the content of the nuclear-encoded subunit COX4 in cardiac mitochondria are reduced in 21-d-old offspring of Cu-deficient dams. COX1 content is normal in 21-d-old cross-fostered offspring of Cu-deficient dams, but CCO activity and COX4 are reduced
-
additional information
-
rapid isolation of mitochondria from rat heart in the presence of various protein phosphatase inhibitors (in the presence of 25 mM NaF, 5 mM sodium vanadate, 10 nM okadaic acid, 2 mM EGTA, and 0.2% bovine serum albumin) results in CcO kinetics with allosteric ATP-inhibition and phosphorylation of subunit I at serine, threonine, and tyrosine
-
additional information
-
enzyme activity decreases only at the late stage of diabetes which is not normalized by insulin treatment. Activity at room temperature (25°C) as well as at physiological temperature (37°C) is not affected by the diabetic state. At the late stage of diabetes the activity at 37°C decreases by 22%
-
additional information
-
ethanol withdrawal decreases the activity of total COX, COX I, and COX IV. Estrogen treatment (17beta-estradiol) prevents the effects of withdrawal on the activities of total COX and COX IV but not COX I. Neither withdrawal nor 17beta-estradiol alter the protein levels of the subunits
-
additional information
-
15 min of global ischemia leads to the inhibition of COXI synthesis to 56% of control. After 1, 3 and 24 hours of reperfusion, COXI synthesis is inhibited to 46, 50 and 72% of control, respectively. Extent COXIII and COXII/ATPase6 synthesis inhibition is comparable to the extent of COXI synthesis inhibition. No significant changes in COXI mRNA and in both COXI and COXII protein level after ischemia, thus ischemia-reperfusion affects directly mitochondrial translation machinery. Ischemia in duration of 15 min and consequent 1, 3 and 24 hours of reperfusion leads to the inhibition of COX activity to 90.3, 80.3, 81.9 and 83.5% of control, respectively
-
additional information
-
rats exposed to a GSM signal at 6W/Kg show decreased CO activity in some areas of the prefrontal and frontal cortex (infralimbic cortex, prelimbic cortex, primary motor cortex, secondary motor cortex, anterior cingulate cortex areas 1 and 2), the septum (dorsal and ventral parts of the lateral septal nucleus), the hippocampus (dorsal field CA1, CA2 and CA3 of the hippocampus and dental gyrus) and the posterior cortex (retrosplenial agranular cortex, primary and secondary visual cortex, perirhinal cortex and lateral entorhinal cortex). Exposure to GSM at 1.5W/Kg does not affect brain activity
-
additional information
the enzyme is resistant to specific inhibitors of copper-containing oxidases, such as NaN3 and NaF
-
additional information
-
the enzyme is resistant to specific inhibitors of copper-containing oxidases, such as NaN3 and NaF
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3Z)-3-[(4-hydroxy-3,5-dimethoxyphenyl)methylidene]-1-[3-[(5-hydroxy-4-oxo-2-phenyl-4H-1-benzopyran-7-yl)oxy]propyl]-1,3-dihydro-2H-indol-2-one
-
compound developed for clipping cyanide from the enzyme and restoring its normal function. The binding constant with CN- is 230000 per M and its ED50 for restoring the cyanide bound CcOX activity in 10 min is 16 microM. The compound interacts with CN- over the pH range 5-10
Insulin
-
insulin treatment at early stage of diabetes (1-week diabetic animals) results in hyper-stimulation, but it is ineffective in restoring the activity in 1-month diabetic animals
-
phosphatidylinositol
-
2.1fold activation of horse heart cytochrome c mediated reaction, 2.4fold activation of Candida krusei cytchrome c mediated reaction
phosphatidylserine
-
7.2fold activation of horse heart cytochrome c mediated reaction, 4.7fold activation of Candida krusei cytchrome c mediated reaction
poly-L-lysine
-
strong activation of Nitrosomonas europaea cytochrome c oxidation
salicylic acid
-
produces a slight and transient increase in transcript levels of COX19
siRNA
-
knockdown of Cox7c expression in PC-12 cells blunts Cox activity, which is counteracted by caffeine treatment
-
sodium cholate
-
0.5%, activation if horse heart or Candida krusei cytchrome c are used as electron donors
sodium nitroprusside
-
produces a several fold increase in COX19 expression after 4 h of treatment, but transcript levels return to normal values after higher incubation times
sodiumdodecylsulfate
-
0.01%, strong activation if horse heart or Candida krusei cytchrome c are used as electron donors
Surf1
-
biogenesis of mitochondrial cytochrome c oxidase relies on a large number of assembly factors, among them the transmembrane protein Surf1
-
trans-[RuCl2(3,4-pyridinedicarboxylic acid)4]Cl
-
increases COX activity in hippocampus, striatum and cerebral cortex
-
trans-[RuCl2(3,5-pyridinedicarboxylic acid)4]
-
increases COX activity in hippocampus, striatum, cerebral cortex and kidney
Caffeine
increases Cox7c mRNA expression in the male striatum. Cox7c is up-regulated in the striatum of male but not female mice after receiving a single dose of caffeine. Cox1 and Cox4 are also stimulated by caffeine in a male-specific fashion. A2AR-specific agonist 2-[p-(2-carboxyethyl)phenethylamino]-5'-N-ethylcarboxamidoadenosine counteracts the elevation of Cox expression and activity by caffeine
Caffeine
-
increases Cox7c mRNA expression in PC-12 cells. This occurrs at the level of transcription and is mediated by a segment of the Cox7c promoter
cardiolipin
-
stimulation of reaction with horse ferrocytochrome c, reactivity with cytochrome c550 is not affected
cardiolipin
-
activation if horse heart or Candida krusei cytchrome c are used as electron donors
Cox17p
-
activation may not be essential to the progress of embryogenesis before gastrulation
-
Cox17p
-
Cox17p specifically binds Cu(I) at a molar copper content of 3.3 under redzuced conditions and significantly activates the mitochondrial. The Cu-Cox17p complex is maintained between pH values from 5.0 to 7.7. Cu is completely released from Cox17p at pH 8.0. The stringent selectivity of Cox17p for cipper is required for enzyme activation
-
NO
-
geminates recombination in mitochondrial CcO. Can accommodate only one NO molecule in its active site
NO
-
is able to bind two NO molecules in its active site. NO is expected to have only a marginal regulatory role at the level of CcO aa
phosphatidylcholine
-
2.7fold activation of horse heart cytochrome c mediated reaction, 3fold activation of Candida krusei cytchrome c mediated reaction
Tween-20
-
the CcO activity of rat liver and heart mitochondria in the presence of 5 mM ADP increases with increasing Tween-20 concentrations. With rat liver mitochondria almost no CcO activity is found in the absence of Tween-20 in contrast to heart mitochondria, where about 50% of maximal activity is measured. Maximal activity rates are measured between 0.5% and 2% (v/v) Tween-20
additional information
-
mechanism of antibody-induced stimulation of COX electron transfer activity. Subunit III is conformationally linked to the redox centers in subunit I of the enzyme. Antibody binding to subunit III perturbs the interaction of subunit III with subunit I to cause an increase in electrin transfer rate
-
additional information
-
decreasing pH from 8.0 to 6.4 is accompanied by a 5fold increase of cytochrome oxidase activity
-
additional information
-
tridentate cross-linked histidine-phenol Cu(II) ether and ester complexes as chemical analogs of the active site
-
additional information
-
arachidonic acid, cholic acid and CHAPS have no effect on the activity of wild-type CcO
-
additional information
-
overexpression of subunit Vb increases COX activity and decreases reactive oxygen species production in wild-type HeLa-20 cells, along with some increase in tolerance to hyperoxia
-
additional information
-
overexpression of the NF-YA/B/C transcription complex in SURF1-deficient fibroblasts from an Leighs syndrome patient efficiently rescues their COX deficiency
-
additional information
-
segments of human skeletal muscle fibers harboring two pathogenic mitochondrial DNA mutations retain normal COX activity by maintaining a minimum amount of wild-type mitochondrial DNA
-
additional information
-
chronic high-frequency stimulation of the subthalamic nucleus increases COI mRNA expression, suggesting global activation of globus pallidus internalis neurons
-
additional information
-
protein kinase C epsilon activates under hypoxic conditions. CytCOx activity is increased by 5fold after hypoxia. Under normoxic conditions, in whole lenses, there is only a weak interaction between protein kinase C epsilon and CytCOx
-
additional information
-
no activation with Tween 20, Triton X-100 or phosphatidylcholin
-
additional information
-
CcO immobilized on a metal film can be activated by cytochrome c oxidation/reduction
-
additional information
-
activity of cytochrome-c oxidase from heart is 2-7fold increased when the membrane integrity is disrupted by hypotonic swelling, freeze-thawing, or a detergent
-
additional information
-
after administering NaN3, chronic treatment with ladostigil prevents the decrease in choline acetyltransferase in the diagonal band, the compensatory increase in synaptic plasticity and transferrin receptors and the memory deficits without restoring COx activity
-
additional information
-
haloperidol, clozapine, olanzapine, or aripiprazole do not alter COX
-
additional information
-
ischemic preconditioning administered before prolonged ischemia-reperfusion induces a 1.9fold increase in coimmunoprecipitation of cytochrome oxidase subunit IV, with anti-PKC-epsilon antisera and a 2fold enhancement of cytochrome-c oxidase activity. Intact mitochondria show virtually no cytochrome-c oxidase activity, unless they are permeablized with n-dodecyl-beta,D-maltoside
-
additional information
-
overexpression of Hap4p, the catalytic subunit of the CCAAT binding transcriptional activator Hap2/3/4/5p complex, suppresses the respiratory defect of yeast shy1 mutants by increasing the expression of nuclear-encoded COX subunits that interact with the mitochondrially encoded Cox1p
-
additional information
-
synthetic models of the active site of cytochrome c oxidase [(LN4-OH)CuI-FeII(TMP)]+ and [(LN3-OH)CuI-FeII(TMP)]+
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
ferrocytochrome c
-
biphasic kinetic with 2 different Km values
0.00005
ferrocytochrome c
-
high affinity Km, kidney, heart, and muscle enzyme, at 27 mM ionic strength
0.00007
ferrocytochrome c
-
high affinity Km, liver enzyme, at 27 mM ionic strength
0.00012
ferrocytochrome c
-
heart enzyme, high affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid
0.00016
ferrocytochrome c
-
liver enzyme, high affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid
0.00071
ferrocytochrome c
-
heart enzyme, low affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid
0.00126
ferrocytochrome c
-
2 Km values for horse heart, Neurospora crassa, Saccharomyces cerevisiea and Candida krusei cytochrome c
0.0013
ferrocytochrome c
-
horse heart cytochrome c, chymotrypsin treated enzyme
0.00132
ferrocytochrome c
-
horse heart cytochrome c, high-affinity Km, 30 mM ionic strength
0.00148
ferrocytochrome c
-
liver enzyme, low affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid
0.0017
ferrocytochrome c
-
horse heart cytochrome c, in the presence of 0.1% Triton X-100 and 2 mg/ml asolectin, chymotrypsin treated enzyme
0.0018
ferrocytochrome c
-
horse cytochrome c, in the presence of cardiolipin
0.0021
ferrocytochrome c
-
horse heart cytochrome c, in the presence of 0.1% Triton X-100 and 2 mg/ml asolectin
0.0037
ferrocytochrome c
-
Candida krusei cytochrome c, in the presence of cardiolipin
0.0038
ferrocytochrome c
-
horse cytochrome c, in the presence of cardiolipin
0.004
ferrocytochrome c
-
biphasic kinetic with 2 different Km values
0.006 - 0.077
ferrocytochrome c
-
dependency on pH, phosphate and K+ concentration
0.015
ferrocytochrome c
-
yeast cytochrome c, in the presence of 100 mM KCl
0.0153
ferrocytochrome c
-
horse heart cytochrome c, 100 mM ionic strength
0.016
ferrocytochrome c
-
horse heart cytochrome c, in the presence of 50 mM KCl
0.026
ferrocytochrome c
-
oxidation of bovine or yeast cytochrome c
0.0407
ferrocytochrome c
-
28°C, presence of 3 mM ADP, pH not specified in the publication
0.13
ferrocytochrome c
-
horse heart cytochrome c, low-affinity Km, 30 mM ionic strength
0.003
ferrocytochrome c550
-
Magnetospirillum magnetotacticum cytochrome c550
-
0.067
ferrocytochrome c551
-
cytochrome c551 from thermophilic bacterium PS3
-
0.000023
reduced cytochrome c551
-
mutant enzyme E116Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000026
reduced cytochrome c551
-
wild type enzyme, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000035
reduced cytochrome c551
-
mutant enzyme E84Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000044
reduced cytochrome c551
-
mutant enzyme D49N, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000059
reduced cytochrome c551
-
mutant enzyme E66Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000063
reduced cytochrome c551
-
mutant enzyme E139Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000074
reduced cytochrome c551
-
mutant enzyme E68Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.0001
reduced cytochrome c551
-
mutant enzyme E64Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
0.000154
reduced cytochrome c551
-
mutant enzyme D99N, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
additional information
additional information
-
enzyme exhibits positive cooperativity at low ionic strength, increasing the KCl concentration to 25 mM causes loss of cooperativity
-
additional information
additional information
-
comparison of high and low affinity Km values at low ionic strength with Rhodobacter spaeroides and horse cytochrome c of wild-type and various mutants
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24.3
phenazine methosulfate
-
ascorbate/phenazine methosulfate assay system
4 - 5
ferrocytochrome c
-
Saccharomyces cerevisiae cytochrome c, in the presence of 0.05% laurylmaltoside
5 - 7
ferrocytochrome c
-
Saccharomyces cerevisiae cytochrome c, in the presence of asolectin
6
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, W143A mutant enzyme
8 - 12
ferrocytochrome c
-
in the presence of 0.1% dodecyl-beta-D-maltoside
13.3 - 16
ferrocytochrome c
-
enzyme reconstituted into asolectin liposomes
14
ferrocytochrome c
-
Candida krusei cytochrome c, in the presence of cardiolipin
20
ferrocytochrome c
-
Thiobacillus novellus cytochrome c, 12.5 mM phosphate at pH 5.5 and 20°C
20
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, W143F mutant enzyme
32
ferrocytochrome c
-
horse cytochrome c, in the presence of cardiolipin
45.8
ferrocytochrome c
-
Candida krusei cytochrome c, 30 mM phosphate at pH 5.5 and 20°C
50
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, D229N mutant enzyme
54
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, D195Q mutant enzyme
100
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, E157Q and E254A mutant enzyme
111
ferrocytochrome c
-
Crithidia fasciculata cytochrome c, very low turnover numbers with human, yeast, rat, horse, and bovine cytochrome c
180
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, D214N mutant enzyme
220
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, D151N/E152Q mutant enzyme
230
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, E148Q mutant enzyme
260
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, D188N/E189Q mutant enzyme
270
ferrocytochrome c
-
Rhodobacter sphaeroides cytochrome c, wild-type enzyme
290
ferrocytochrome c
-
wild-type enzyme, horse cytochrome c, 155 mM ionic strength
336
ferrocytochrome c
-
horse cytochrome c, in the presence of cardiolipin
400
ferrocytochrome c
-
horse cytochrome c, D214N and D229N mutant enzyme
550
ferrocytochrome c
-
reconstituted recombinant D407C mutant enzyme
590
ferrocytochrome c
-
wild-type enzyme, horse cytochrome c, 5 mM ionic strength
600
ferrocytochrome c
-
horse cytochrome c, E157Q and E254Amutant enzyme
700
ferrocytochrome c
-
reconstituted recombinant D407A mutant enzyme
700
ferrocytochrome c
-
reconstituted recombinant D407N mutant enzyme
980
ferrocytochrome c
-
wild-type, D188N/E189Q and D151N/E152Q mutant enzyme, horse cytochrome c, 75 mM ionic strength
1300
ferrocytochrome c
-
horse cytochrome c, D151N/E152Q mutant enzyme
1600
ferrocytochrome c
-
horse cytochrome c, D188N/E189Q mutant enzyme
37.4
ferrocytochrome c550
-
Magnetospirillum magnetotacticum cytochrome c550
-
3.93
N,N,N',N'-tetramethyl-4-phenylendiamine
-
ascorbate/N,N,N',N'-tetramethyl-p-phenylendiamine assay system
-
60
N,N,N',N'-tetramethyl-4-phenylendiamine
-
ascorbate/N,N,N',N'-tetramethyl-p-phenylendiamine assay system
-
30
reduced cytochrome c551
-
mutant enzyme E116Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
140
reduced cytochrome c551
-
mutant enzyme D99N, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
199
reduced cytochrome c551
-
mutant enzyme E66Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
200
reduced cytochrome c551
-
mutant enzyme D49N, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
290
reduced cytochrome c551
-
mutant enzyme E68Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
295
reduced cytochrome c551
-
wild type enzyme, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
297
reduced cytochrome c551
-
mutant enzyme E139Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
317
reduced cytochrome c551
-
mutant enzyme E64Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
325
reduced cytochrome c551
-
mutant enzyme E84Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8
-
additional information
additional information
-
kcat increases with decreasing pH
-
additional information
additional information
-
above 20 mM phosphate: rapid decrease of kcat with Candida krusei, tuna, Thiobacillus novellus, and horse cytochrome c
-
additional information
additional information
-
highest turnover number at 55 mM ionic strength: D214N, D195N and E148Q, highest turnover number at 45 mM ionic strength: E157Q, comparison of high and low affinity turnover numbers at low ionic strength with Rhodobacter spaeroides and horse cytochrome c of wild-type and various mutants
-
additional information
additional information
-
study of reaction kinetics assuming a fast protonic phase with a proton transfer to H291 and a slow process with a proton transfer to OH-group of binuclear catalytic site. Comparison with kinetics of enzyme from Paracoccus denitrificans and Bos taurus
-
additional information
additional information
-
study of reaction kinetics assuming a fast protonic phase with a proton transfer to H291 and a slow process with a proton transfer to OH-group of binuclear catalytic site. Comparison with kinetics of enzyme from Rhodobacter spaeroides and Bos taurus
-
additional information
additional information
-
study of reaction kinetics assuming a fast protonic phase with a proton transfer to H291 and a slow process with a proton transfer to OH-group of binuclear catalytic site. Comparison with kinetics of enzyme from Rhodobacter spaeroides and Paracoccus denitrificans
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.015
0.05
111
-
purified enzyme, pH 7.0, 25°C, N,N,N',N'-tetramethyl-p-phenylene diamine oxidase activity
147
4
-
initial membrane fraction, pH 7.0, 25°C, N,N,N',N'-tetramethyl-p-phenylene diamine oxidase activity
additional information
additional information
-
CuA depleted enzyme shows 15% activity of native and 75% activity of p-(hydroxymercuri)benzoate modified enzyme
additional information
-
spectra of the A, PM, F and O inermediate 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
additional information
-
activity of cytochrome-c oxidase from heart is 2-7fold increased when the membrane integrity is disrupted by hypotonic swelling, freeze-thawing, or a detergent
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
6.1
6.5
7 - 7.6
-
oxidation of {N,N,N,N-tetramethyl-p-phenylenediamine
7.4
5.6
-
oxidation of Candida krusei and Saccharomyces oviformis cytochrome c
6
-
oxidation of Magnetospirillum magnetotacticum cytochrome c550
6.5
-
wild-type, D407A, D407C and D407N mutant enzyme, sharp drop above
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
recombinant enzyme expressed in Escherichia coli, comparison with human and Arabidosis thaliana enzyme
-
-
brenda
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
brenda
Accession number of subunit 2 of Aa3 oxidase
UniProt
brenda
Q5GCA8 i.e. catalytic subunit CcoN, Q5GCA7 i.e. subunit CcoO, Q5GCA5 i.e. subunit CcoP, Q5GCA6 i.e. subunit CcoQ
Q5GCA8; Q5GCA7; Q5GCA5; Q5GCA6
UniProt
brenda
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
-
-
brenda
-
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
-
-
brenda
-
P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184
UniProt
brenda
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
-
-
brenda
-
395028, 395996, 396079, 396120, 396122, 396130, 657924, 657937, 657975, 658073, 672022, 672108, 672326, 672354, 674434, 690895, 691023, 694959
-
-
brenda
-
395991, 395992, 395994, 395997, 396000, 396001, 396002, 396005, 396007, 396008, 396012, 396013, 396050, 396057, 396100, 396109, 396110, 700992
-
-
brenda
-
674427, 674791, 675018, 675528, 675538, 688882, 690326, 691050, 691404, 692575, 692992, 698934, 724411, 742002, 743020
-
-
brenda
patients with mutations in genes SCO2 or SURF1 affecting enzyme assembly
-
-
brenda
recombinant enzyme expressed in Escherichia coli, comparison with Arabidopsis thaliana and horse enzyme
-
-
brenda
-
658633, 659932, 692264, 692992, 694387, 694987, 695140, 697203, 699003, 699664, 700420, 742002, 742243
-
-
brenda
-
395028, 395991, 395995, 395996, 396003, 396034, 396042, 396044, 396060, 396134, 396137, 658057, 671947, 672326, 691038, 691335, 693008, 725643, 741886, 741953
-
-
brenda
-
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
-
-
brenda
-
396002, 396004, 396006, 396058, 396072, 396093, 396094, 396095, 396116, 692985, 700002, 752804, 755489
-
-
brenda
all 44 partially or totally sequenced cyanobacterial genomes are analyzed for the occurence of cytM and its putative electron acceptor cytochrome c oxidase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
cortical astrocyte. Differential, cell-type specific expression of enzyme subunit IV isoform 2 in cortical astrocytes and cerebellar neurons. Presence of subunit IV isoform 2 suppresses the sensitivity of enzyme to its allosteric regulator ATP and overrules the regulation by the cellular energy level. Pivotal role of enzyme as an oxygen sensor in brain
brenda
-
primary cardiac cell culture of neonatal rats, increase in enzyme activity by interaction of enzyme subunit IV with protein kinase Cepsilon upon hypoxia
brenda
-
expression in leaves is only observed when cuts are produced, suggesting an induction by wounding
brenda
-
comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity in different types of muscle
brenda
-
comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity in different types of muscle
brenda
-
superficial and deep semimembranosus, comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity in different types of muscle
brenda
-
comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity in different types of muscle
brenda
additional information
-
cytochrome-c oxidase activity is abnormal in cerebellar cortex, dentate nucleus, and brainstem regions of Girk2(Wv) (Weaver) mutant mice. Metabolic alterations in cerebellar and vestibular regions are linearly correlated with poor motor coordination
brenda
-
-
brenda
cerebellar neurons. Differential, cell-type specific expression of enzyme subunit IV isoform 2 in cortical astrocytes and cerebellar neurons. Presence of subunit IV isoform 2 suppresses the sensitivity of enzyme to its allosteric regulator ATP and overrules the regulation by the cellular energy level. Pivotal role of enzyme as an oxygen sensor in brain
brenda
-
regular alternation of areas with high and low levels of activity of the respiratory enzyme CO in layers III, IV, and VI of field 17 and in layers IV and VII of field 18 of the cerebral cortex
brenda
P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184
-
brenda
-
-
395999, 396016, 396019, 396028, 396033, 396035, 396037, 396039, 396040, 396041, 396043, 396049, 396052, 396058, 396063, 396064, 396065, 396067, 396080, 396084, 396092, 396104, 396118, 396126, 657655, 658173, 658620, 659582, 673702, 676865, 691023, 691038, 691404
brenda
P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184
-
brenda
-
-
brenda
-
downregulation of enzyme activity in the neonatal period by factor 3
brenda
-
cells proliferate under 80% O2. Under both 20% and 80% O2, mitochondrial reactive oxygen species production is 2fold less in HeLa-80 cells than in wild-type HeLa cells, related to a 2fold higher cytochrome-c oxidase activity. Elevated enzyme activity is associated with a 2fold increase in the regulatory subunit Vb. Treatment with siRNA against subunit Vb lowers its expression, increases mitochondrial generation of reactive oxygen species, decreases enzyme activity by 60-80% and diminishes viability under 80% O2
brenda
-
elevated COX activity in the oxygen-tolerant HeLa-80 cells, associated with a more than 2fold increase in the regulatory subunit COX Vb, whereas expression levels of other subunits are very close to wild-type HeLa-20 cells
brenda
P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184
-
brenda
-
comparison of enzyme activities in liver of arctic and temperate teleosts. Antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
brenda
-
comparison of enzyme activities in liver of arctic and temperate teleosts. Antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
brenda
-
comparison of enzyme activities in liver of arctic and temperate teleosts. Antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
brenda
-
-
brenda
-
thyroid hormone T3 induces concomitant increase in the protein and mRNA expression of nuclear-encoded subunit COX Vb and produces a significant increase in COX III mRNA
brenda
-
comparison of enzyme activities in liver of arctic and temperate teleosts. Antioxidant enzyme activities may not be enhanced as part of adaptation in arctic fishes, at least not in the liver
brenda
-
psoas major, longissimus lumborum, superficial semimembranosus, deep semimembranosus, and semitendinosus muscle, comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity
brenda
-
highly stained in AtCOX19-1::GUS plants. Activity in roots is already evident at very early stages of development (1-2 days after imbibition), but not in embryos at late stages of embryogenesis and is higher in the root meristem, the vascular cylinder and nascent secondary roots
brenda
-
tetracycline-inducible cell line derived from Flp-InTM TRExTM-293 cells (Invitrogen), stably expressing human nitric oxide synthase
brenda
additional information
-
infection of plants with the pathogenic bacterium Pseudomonas syringae pv. tomato induces COX19 gene expression
brenda
additional information
-
in C1 cells, C2 cells and C3 cells steady state level of complex I is significantly reduced due to a defective assembly of complex IV. Also present in 4A cells
brenda
additional information
-
in the central auditory system cytochrome oxidase activity increases in the granular cell layer of dorsal cochlear nucleus, trapezoid body nucleus, intermediate lateral lemniscus, central and external inferior colliculus, and pyramidal cell layer of primary auditory cortex of Relnrl-Orl (reeler) mutant mice, whereas activity decreases in the superficial molecular layer of dorsal cochlear nucleus as well as in the medioventral periolivary nucleus
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
mitochondrion-endoded subunit COXII does not localize exclusively to mitochondria, but is also present in cytosol. COXIV RNA-binding activity, present in the mitochondrial fraction, decreases during development with inverse correlation with accumulation of COXIV precursor in the cytoplasm
brenda
additional information
-
cytochrome oxidase unilamellar vesicles (COV). Purified COV contains approximately 1 COX molecule per liposome. Purified COV exhibits similar physical properties as unpurified COV
-
brenda
the recombinant protein is found in the cytoplasmic fraction
brenda
-
the recombinant protein is found in the cytoplasmic fraction
-
brenda
-
AtCOX19 isoforms are imported into mitochondria in vitro and are attached to the inner membrane facing the intermembrane space
-
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184
-
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca.2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca.2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca.2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca.2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca.2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca.2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca.2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
the near N-terminus ca. 2/3 of the MCOX2e region contains an interspecifically variable number of predicted transmembrane helices
brenda
P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184
-
brenda
-
-
brenda
-
-
brenda
-
-
657776, 689159, 690357, 693451, 693722, 693787, 694175, 694360, 694379, 694394, 694592, 695076, 695205, 700077, 711289, 712326, 712814, 713547, 742031, 742816, 743634
brenda
-
mitochondrion-endoded subunit COXII does not localize exclusively to mitochondria, but is also present in cytosol. COXIV RNA-binding activity, present in the mitochondrial fraction, decreases during development with inverse correlation with accumulation of COXIV precursor in the cytoplasm
brenda
-
in intact mitochondria, CO binds to two heme proteins, CytcO and flavohemoglobin yHb. yHb resides in the intermembrane space. In vesicles of the inner mitochondrial membranes the only CO-binding protein is CytcO
brenda
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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
-
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
-
T cell cytochrome c oxidase dysfunction results in apoptosis in vitro
malfunction
-
a CcoM deletion strain displays altered growth rates under anaerobic denitrifying conditions
-
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
metabolism
-
the cytochrome c oxidase plays an important role in regulating endogenous nitric oxide concentrations
metabolism
Q5GCA8; Q5GCA7; Q5GCA5; Q5GCA6
sequential assembly model of cbb3 cytochrome c oxidase. The CcoQ subunit is required for the early maturation step, CcoQ first associates with CcoN before the CcoNQ-CcoO interaction. CcoP associates to CcoNQO subcomplex in the late maturation step, and once the CcoNQOP complex is fully formed, CcoQ is released for degradation by the FtsH protease. Under microaerobiosis conditions, the wild-type strain reduces oxygen at a rate of 5.8% of dissolved oxygen/h. The O2 consumption rate is greatly and similarly affected in subunit mutants CcoN, CcoO and CcoP, but only reduced in a mutant lacking CcoQ
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
-
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
-
cytochrome c oxidase regulates activation and proliferation in T cells through apoptosis
physiological function
-
cytochrome c oxidase utilizes a heterobinuclear active site composed of a heme moiety and a mononuclear copper center coordinated to three histidine residues, one of which is covalently cross-linked to a tyrosine. A route employing an iron(III) meso-substituted isoporphyrin derivative is proposed to be a key intermediate in the Tyr-His cofactor biogenesis. Iron(III) meso-substituted isoporphyrins prepared with azide, cyanide, and substituted imidazole functionalities when added to 1,3,5-trimethoxybenzene lead to formation of an organic product containing the imidazole coupled to aromatic substrate via a new C-N bond
physiological function
-
mitochondrial glycerol 3-phosphate oxidation is controlled by adenylates through allosteric regulation of cytochrome c oxidase (COX) activity in flight muscle. ADP significantly activates respiratory rates linked to glycerol 3-phosphate oxidation, in a protonmotive force-independent manner. ADP activates respiration through a slightly cooperative mechanism. COX activity ias allosterically activated by ADP. ATP exerts powerful inhibitory effects on respiratory rates linked to glycerol 3-phosphate oxidation and on COX activity
physiological function
-
the respiratory supercomplex factor Rcf 1 binds to intact cytochrome c oxidase. Removal of Rcf1 yields two CytcO sub-populations. One of these sub-population displays unperturbed absorption spectra, CO-recombination kinetics and internal electron transfer. In the other population, the midpoint potential of the catalytic site is lowered and CO recombination is accelerated
physiological function
Saccharomyces cerevisiae W303a
-
the respiratory supercomplex factor Rcf 1 binds to intact cytochrome c oxidase. Removal of Rcf1 yields two CytcO sub-populations. One of these sub-population displays unperturbed absorption spectra, CO-recombination kinetics and internal electron transfer. In the other population, the midpoint potential of the catalytic site is lowered and CO recombination is accelerated
-
physiological function
-
CcoM plays a role in anaerobic respiration
-
Show AA Sequence and Transmembrane Helices (1746977 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
10068
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
10670
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
11000
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
115000
11600
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
12000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
12436
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
12627
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
13000
13700
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
14000
140000 - 158000
14570
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
14858
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
17074
-
1 * 60371 + 1 * 17074 + 1 * 5976, calculated from amino acid sequence
17153
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
17500
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
17900
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
18000
180000 - 280000
-
minimal molecular weight, calculated from subunit composition, heme content
19000
20000
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
200000
20100
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
21000
210000
22000
226000
-
estimated from sucrose density gradient centrifugation and gel filtration
23000
23100
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
26000
26049
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
26678
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
28000
29000
290000 - 315000
29500
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
29918
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
30000
30340
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
31000
32000
33000
33500
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
34000
35000
35100
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
37000
38000
39000
40000
43000
43600
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
45000
50000
5364
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
5441
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
55000
5600
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
56000
56993
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
5700
57000
58000
-
1 * 58000 + 1 * 26000, 58000 Da band may be composed of 2 subunits of the cb-type oxidase, the 26000 Da subunit may be a heme c bearing diheme or mono-heme of the enzyme, SDS-PAGE
5976
-
1 * 60371 + 1 * 17074 + 1 * 5976, calculated from amino acid sequence
6000
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
60371
-
1 * 60371 + 1 * 17074 + 1 * 5976, calculated from amino acid sequence
6244
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
6303
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
6350
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
6603
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
71000
8480
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
8750
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
8800
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
9000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
9419
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
9500
13000
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
13000
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
14000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
18000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
19000
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
200000
-
heart, monomeric enzyme, deoxycholate solubilized, hydrodynamic measurements
21000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
210000
-
vertebrate, theoretical value of monomer composed of 12-13 different subunits
22000
-
1 * 56000 + 1 * 38000 + 1 * 22000, SDS-PAGE, Ferguson plot
23000
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
26000
-
1 * 58000 + 1 * 26000, 58000 Da band may be composed of 2 subunits of the cb-type oxidase, the 26000 Da subunit may be a heme c bearing diheme or mono-heme of the enzyme, SDS-PAGE
26000
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
28000
-
1 * 43000 + 1 * 34000 + 1 * 28000, SDS-PAGE, 5% 2-mercaptoethanol
29000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
32000
-
1 * 55000 + 1 * 32000, SDS-PAGE, immunoblotting
34000
-
1 * 71000 + 1 * 34000, subunit I shows anomalous behaviour on SDS-PAGE, Ferguson plot
34000
-
1 * 43000 + 1 * 34000 + 1 * 28000, SDS-PAGE, 5% 2-mercaptoethanol
34000
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
38000
-
1 * 56000 + 1 * 38000 + 1 * 22000, SDS-PAGE, Ferguson plot
39000
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
40000
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
43000
-
1 * 43000 + 1 * 34000 + 1 * 28000, SDS-PAGE, 5% 2-mercaptoethanol
55000
-
1 * 55000 + 1 * 32000, SDS-PAGE, immunoblotting
55000
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
56000
-
1 * 56000 + 1 * 38000 + 1 * 22000, SDS-PAGE, Ferguson plot
56000
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
5700
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
5700
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
71000
-
1 * 71000 + 1 * 34000, subunit I shows anomalous behaviour on SDS-PAGE, Ferguson plot
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotrimer
homodimer
homotrimer
monomer
oligomer
tetramer
trimer
additional information
?
-
x * 55000 + x * 29500 + x * 19000 + x * 13000 + x * 11000 + x * 5700, homolog to eukaryotic subunit III is lost during purification, SDS-PAGE
?
-
I, II, III, IV, V, x * 39000 + x * 33500 + x * 26000 + x * 20000 + x * 5700, probably 2 more small subunits, SDS-PAGE
dimer
-
1 * 58000 + 1 * 26000, 58000 Da band may be composed of 2 subunits of the cb-type oxidase, the 26000 Da subunit may be a heme c bearing diheme or mono-heme of the enzyme, SDS-PAGE
dimer
-
1 * 55000 + 1 * 32000, SDS-PAGE, immunoblotting
dimer
-
1 * 46000-55000 + 1 * 29000-32000, SDS-PAGE, immunoblotting
dimer
-
1 * 71000 + 1 * 34000, subunit I shows anomalous behaviour on SDS-PAGE, Ferguson plot
heterotrimer
-
1 * 60371 + 1 * 17074 + 1 * 5976, calculated from amino acid sequence
heterotrimer
-
1 * 60371 + 1 * 17074 + 1 * 5976, calculated from amino acid sequence
-
oligomer
-
I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences
oligomer
-
I, II, III, IV, V, VI, VII, 1 * 43600 + 1 * 20100 + 1* 18000 + 1 * 13700 + 1 * 8800 + 1 * 5600 + 1 * 3700, SDS-PAGE
oligomer
-
I, II, III, IV, V, VI, VII, 1 * 40000 + 1 * 29000 + 1 * 21000 + 1 * 18000 + 1 * 14000 + 1 * 12000 + 1 * 9000, proposed subunit composition, stoichiometry
oligomer
-
I, II, III, IV, Va, Vb, VIIa, VIIc, VIII, 1 * 56000 + 1 * 26678 + 1 * 30340 + 1 * 14858 + 1 * 12627 + 1 * 14570 + 1 * 6603 + 1 * 5364 + 1 * 6303, amino acid sequences
oligomer
-
I, II, III, IV, V, VI, VII, 1 * 34000 + 1 * 23000 + 1* 20000 + 1 * 17500 + 1 * 13000 + 1 * 10000 + 1 * 6000, SDS-PAGE
oligomer
-
I, II, III, IV, V, VI, VII, 1 * 35100 + 1 * 23100 + 1* 21300 + 1 * 17900 + 1 * 11600 + 1 * 8750 + 1 * 4600, possibly multiple subunits at position VII, SDS-PAGE
trimer
-
1 * 56000 + 1 * 38000 + 1 * 22000, SDS-PAGE, Ferguson plot
trimer
-
1 * 43000 + 1 * 34000 + 1 * 28000, SDS-PAGE, 5% 2-mercaptoethanol
additional information
-
composed of more than 10 different protein subunits
additional information
-
X-ray data: subunits form a dimeric quarternary structure that may also exist under physiological conditiones
additional information
-
differences in small subunit composition depending on source of enzyme
additional information
-
subunit structure, arrangement of subunits in enzyme complex
additional information
-
sequence alignments of subunits I, II and III of various eukaryotic and prokaryotic organisms
additional information
-
hydrophilic domains of COX subunit III are conformationally linked to the electron transfer function of the enzyme in subunit I and II. Subunit III may serve as a regulatory subunit for COX electron transfer and proton pumping activities
additional information
dilution of the purified protein causes dissociation of the dimer to the monomer. When the pH is raised to 7.4 or 8.5, the protein also shifts from the dimer to the monomer. In solution, CcO is in an equilibrium state between the dimer and monomer
additional information
-
dilution of the purified protein causes dissociation of the dimer to the monomer. When the pH is raised to 7.4 or 8.5, the protein also shifts from the dimer to the monomer. In solution, CcO is in an equilibrium state between the dimer and monomer
additional information
-
enzyme complex lacking subunit III exhibits a shorter catalytic life span and absence of subunit III dramatically slows proton uptake to the active site via the D proton pathway. Arachidonic acid stimulates proton uptake by the D pathway and retards suicide inactivation. Average catalytic life span of detergent-solubilized complex lacking subunit III decreases dramatically with pH. Maintenance of rapid proton transfer through the D pathway and the backflow/exit pathway is one mechanism by which subunit III normally functions to prevent uicide inactivation of cytochrome c oxidase
additional information
-
approx. 10 different subunits after 2D gel electrophoresis
additional information
-
it is suggested that the mitochondrial encoded subunits I, II and III are the catalytic core of the enzyme
additional information
-
copper-binding protein SCO1 is involved in the assembly of mitochondrial cytochrome-c oxidase. It functions not as a cytochrome-c oxidase copper chaperone, but rather as a mitochondrial redox signaling molecule
additional information
-
brain enzyme from swayback-diseased animals is deficient of subunits II, III and IV
additional information
-
13 different subunits in 1/1 stoichoimetric amounts
additional information
-
fetal enzyme complex differs from adult heart complex by migration differences of subunits VIa and VIII
additional information
-
the enzyme is built up with both nucleus and mitochondrion-encoded subunits
additional information
-
upon exposure of cells to hypoxia, enzyme subunit IV interacts with protein kinase Cepsilon resulting in increase in cytochrome c oxidase activity
additional information
-
enzyme complex contains eleven rather than twelve subunits
additional information
-
subunits I, II, and III detected by immunoblotting, a mitochondria-like subunit IV that may confer allosteric properties to the enzyme is also suggested
additional information
-
subunits I, II, and III detected by immunoblotting, a mitochondria-like subunit IV that may confer allosteric properties to the enzyme is also suggested
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
subunit III binds two lipids within a deep cleft. Altering the lipid binding sites mimics a major loss of subunit III, even though subunit III is completely retained, in that suicide inactivation becomes much more probable
phospholipoprotein
phosphoprotein
-
cAMP-dependent tyrosine phosphorylation of subunit I inhibits cytochrome c oxidase activity
additional information
additional information
-
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
additional information
covalent link between Y311 and the copper-ligating histidine residue
additional information
-
covalent link between Y311 and the copper-ligating histidine residue
additional information
-
thyroid hormone T3 regulates the expression of COX subunits by both transcriptional and posttranslational mechanism
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
concentration of the purified enzyme by Amicon ultrafiltration in 0.3-1 mM or 10 mM sodium phosphate buffer, dimeric in crystal lattice
-
enzyme from heart can be crystallized in hexagonal, tetragonal and orthorhombic forms
-
microbatch method, at pH 7.3 and 5.7, using 3% (w/v) polyethylene glycol 1500 as precipitant
-
monomeric bovine cytochrome c oxidase with bound cytochrome c, microbatch method
-
oxidized and reduced structures of monomer with resolutions of 1.85 and 1.95 A, respectively. A hydrogen bond network of water molecules is formed at the entry surface of the proton transfer pathway, in monomeric CcO, whereas this network is altered in dimeric CcO. Phospholipid structures are found with the protein complex, two cardiolipins are found at the interface region of the supercomplex
room temperature, pH 6.8, damage-free structure in the carbon monoxide-bound state at a resolution of 2.3 A. In the femtosecond X-ray crystallography structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of about 142°. In the synchrotron structure, the Fe-CO bond is cleaved. CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by about 0.38 Å. Ligand binding to the heme a3 iron in the femtosecond X-ray crystallography structure is associated with an allosteric structural transition
two-dimensional crystals by insertion of the enzyme into preformed lipid vesicles
-
sitting drop vapor diffusion method, using 0.058% (w/v) n-undecyl-alpha-D-maltoside, 0.125% (w/v) decanoylsucrose and 0.018% (w/v) n-dodecyl-alpha-D-maltoside with pentaerythritol ethoxylate 15/04, ammonium formate, and ammonium tartrate
-
sitting drop vapour diffusion, 200 mM Zn acetate, 100 mM Na acetate, pH 4.5, 19-22% polyethylene glycol 1000, 10 mg/ml enzyme concentration, hexagonal red crystals appear after 3 d at 20°C
-
hanging-drop vapour-diffusion method, X-ray quality crystals are generated and the structure is solved to a resolution of 2.4 A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A205T
-
mutation in subunit III associated with mitochondrial disease, no change in subunit composition of the complex
D132A
-
mutation of initial proton acceptor of the D pathway. Average catalytic life span of D132A complex lacking subunit III is 2-fold to 50-fold less than that of wild-type complex lacking subunit III, depending upon pH, and the catalytic life span of D132A complex lacking subunit III is independent of external pH from pH 6.2 to pH 7.4
D132A/R481K
-
catalytic life span of D132A/R481K holo complex is 10fold shorter than that of wild-type holo complex
D132N
-
proton donor E286 is present, but its reprotonation from the N side of the membrane is blocked
D407A
-
similar properties as wild type, suggesting that D407 does not play a role in proton translocating
D407C
-
similar properties as wild type, suggesting that D407 does not play a role in proton translocating
D407N
-
similar properties as wild type, suggesting that D407 does not play a role in proton translocating
D485A
-
mutant enzyme is active, binds to Ca2+ reversibly, and exhibits the red shift in the heme a absorption spectrum upon Ca2+ binding for both reduced and oxidized states of heme a. Sodium ions reverse the Ca2+-induced red shift of heme a and dramatically decrease the rate of Ca2+ binding to the mutant enzyme. With the mutant enzyme, 1 Ca2+ competes with 1 Na+ for the binding site
E101A
E101A/H96A
-
exhibits low activity and eliminates metal binding at this site. Significant activity is restored by adding lipophilic carboxylic compounds (arachidonic acid and cholic acid), but not by their non-carboxylic analogues. Activity is still inhibited by zinc, but this remaining inhibition is nearly eliminated by removal of subunit III
E101C
-
mutation in subunit II strongly reduces oxidase activity to 8%
E101D
-
mutation in subunit II strongly reduces oxidase activity to 16%
E101H
-
mutation in subunit II strongly reduces oxidase activity to 19%
E101I
-
mutation in subunit II strongly reduces oxidase activity to 8%
E101N
-
mutation in subunit II strongly reduces oxidase activity to 17%
E101Q
-
mutation in subunit II strongly reduces oxidase activity to 14%
E286A/I112E
-
about 2% of wild-type activity in the holo complex, mutant complex lacking subunit III exhibits a very short average catalytic life span of approximately 100 catalytic cycles
E286D
-
mutation in D pathway. E286D complex lacking subunit III exhibits a 75% decrease in its O2 reduction activity, compared to wild-type complex lacking subunit III. Catalytic life span of detergent-solubilized E286D complex lacking subunit III is half that of wild-type complex lacking subunit III or about the same as D132A complex lacking subunit III
E286Q
-
absence of both protonic phases in enzyme kinetics. Mutant is not able to generate the ferryl-oxo form under the experimental conditions applied
F86A
-
mutation in subunit III, results in an enzyme complex that contains only about 50-70% of subunit III compared with wild-type
F93A
-
mutation in subunit III, results in an enzyme complex that contains only about 40-60% of subunit III compared with wild-type
G78S
-
mutation in subunit III associated with mitochondrial disease, no change in subunit composition of the complex
H260N
-
mutant of CuA center, the rate constant for the intramolecular electron transfer from heme c to CuA is decreased from 40000 per s for the wild-type enzyme to 11000 for the mutant enzyme, the rate constant for intracomplex electron transfer from CuA to heme a is decreased from 90000 per s for wild-type enzyme to 45 per s for the mutant. The rate constant for the reverse reaction, heme A to CuA, is 180 per s for the mutant enzyme, compared to 17000 for the wild-type enzyme. The redox potential of CuA is increased by 90 mV relative to hemeA
K362M
L145A/L196A/L203A
-
mutation in subunit I at sites in contact with the fatty acid tails of subunit III, no effect on the content of subunit III in the complex
M263L
-
mutant of CuA center, the rate constant for the intramolecular electron transfer from heme c to CuA is decreased from 40000 per s for the wild-type enzyme to 16000 for the mutant enzyme, the rate constant for intracomplex electron transfer from CuA to heme a is decreased from 90000 per s for wild-type enzyme to 4000 per s for the mutant. The rate constant for the reverse reaction, hemeA to CuA, is 66000 per s for the mutant enzyme, compared to 17000 for the wild-type enzyme. The redox potential of CuA is increased by 120 mV relative to hemeA
M55A
-
mutation in subunit III, results in an enzyme complex that contains only about 30-50% of subunit III compared with wild-type
N139C
in this mutants, proton back leakage through the D-channel is kinetically favored over proton pumping due to the loss of a kinetic gate in the N139 region
N139D
-
turnover rate is increased by a factor of 2-3, mutant does not pump protons
N139L
in this mutant, the bulky L139 side chain inhibits timely reprotonation of E286 through the D-channel, which impairs both proton pumping and the chemical reaction
N139T
in this mutants, proton back leakage through the D-channel is kinetically favored over proton pumping due to the loss of a kinetic gate in the N139 region
R137A
-
mutation in subunit I, results in an enzyme complex that contains only about 5-25% of subunit III compared with wild-type
R226A
-
mutation in subunit III, results in an enzyme complex that contains only about 90% of subunit III compared with wild-type
R481K
-
mutant retains substantial activity and is able to pump protons, but at somewhat reduced rates and stoichiometry
R482A
-
mutant retains substantial activity and is able to pump protons, but at somewhat reduced rates and stoichiometry
R482K
-
mutant retains substantial activity and is able to pump protons, but at somewhat reduced rates and stoichiometry
R482P
-
mutant enzyme is perturbed in its structure and is altered in the redox potential difference between heme a and CuA: 18 mV for R482P compared to +46 mV for the wild-type (hemea - CuA). The electron tranport rate between CuA and heme A is also altered from 93000 per s in the wild-type to 50 per s in the oxidized R482P mutant
R482Q
-
mutant retains substantial activity and is able to pump protons, but at somewhat reduced rates and stoichiometry
S200V/S201V
in the double mutant, the proton affinity of E286 is increased, which slows down both proton pumping and the chemical catalysis
S89A
-
mutation in subunit III, loss of side-chain interaction between S89 and F86 does not affect assembly of the enzyme complex
T359A
-
mutation of K pathway. Steady-state activity of T359A complex lacking subunit III is 20% that of wild-type complex lacking subunit III, and life span is similar to wild-type
W58A
-
mutation in subunit III, results in an enzyme complex that contains only about 50-70% of subunit III compared with wild-type
W59A
-
mutation in subunit III, results in an enzyme complex that contains only about 50-70% of subunit III compared with wild-type
W59A/F86A
-
mutation in subunit III, results in an enzyme complex that contains only about 60-80% of subunit III compared with wild-type
Y311F
no enzymic activity, protein complex is correctly assembled
D49N
-
the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
D99N
-
the mutant shows strongly increased Km and reduced kcat values compared to the wild type enzyme
E116Q
-
the mutant shows slightly reduced Km and strongly reduced kcat values compared to the wild type enzyme
E139Q
-
the mutant shows increased Km and slightly increased kcat values compared to the wild type enzyme
E64Q
-
the mutant shows increased Km and kcat values compared to the wild type enzyme
E66Q
-
the mutant shows increased Km and kcat values compared to the wild type enzyme
E68Q
-
the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
E84Q
-
the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
E116Q
-
the mutant shows slightly reduced Km and strongly reduced kcat values compared to the wild type enzyme
-
E139Q
-
the mutant shows increased Km and slightly increased kcat values compared to the wild type enzyme
-
E64Q
-
the mutant shows increased Km and kcat values compared to the wild type enzyme
-
E66Q
-
the mutant shows increased Km and kcat values compared to the wild type enzyme
-
E84Q
-
the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
-
A122T
recurrent missense mutation in mitochondrially encoded cytochrome oxidase I found in a variety of human cancer cells
G6930A
-
nonsense mutation in the mitochondrially encoded complex IV subunit 1 gene, which causes a disruption in the assembly and defective activity of complex VI
D124N
-
subunit I mutant. Reduction of heme a3-CuB is severely impaired, about 0.8 H+ is promptly bound synchronously with the reduction of heme a, followed by a much slower protonation associated with the retarded reduction of the heme a3-CuB site
K354M
-
subunit I mutant. Reduction of heme a3 is totally impaired, overall H+ uptake within 10 s is significantly smaller than in the wild-type
R54M
-
low turnover number, changes in spectral properties of heme a, lowered midpoint redox potential, electron transfer from CuA to heme a is impaired
Y280H
-
catalytic site retains its active configuration that allows O2 binding to heme a3
DELTAW121
-
mutant of the soluble CuA domain, both the coordination structure of the CuA center and the secondary structure of the protein are changed significantly, the electron transfer activity with cytochrome c is inhibited severely
W121L
-
mutant of the soluble CuA domain, both the coordination structure of the CuA center and the secondary structure of the protein are changed significantly, the electron transfer activity with cytochrome c is inhibited severely
W121Y
-
mutant of the soluble CuA domain, stability decreases compared with the wild-type enzyme. The mutant keeps the same secondary structure as the wild-type protein, but can only transfer electrons with cytochrome c at a rate of one-seventh-fold
C30A
-
is growth-compromised on glycerol/lactate. Is compromised in Cu(I) binding
C30A/C62A
-
is growth-compromised. Is more severely compromised than the single C30A mutant. Fails to accumulate in mitochondria. Is compromised in Cu(I) binding
H26A/C30A
-
is growth-compromised. Fails to accumulate in mitochondria. Is compromised in Cu(I) binding
R63T
-
is nonfunctional even when expressed as an IM-tethered Cox19 fusion
C30A
-
is growth-compromised on glycerol/lactate. Is compromised in Cu(I) binding
-
C30A/C62A
-
is growth-compromised. Is more severely compromised than the single C30A mutant. Fails to accumulate in mitochondria. Is compromised in Cu(I) binding
-
additional information
E101A
-
mutation in subunit II strongly reduces oxidase activity to 8%
E101A
-
exhibits low activity and eliminates metal binding at this site. Significant activity is restored by adding lipophilic carboxylic compounds (arachidonic acid and cholic acid), but not by their non-carboxylic analogues
additional information
-
mutant lacking Surf1p involved in assembly of cytochrome-c oxidase shows three subpopulations of enzyme with structurally distinct heme a3-CuB active sites, 50% of enzyme lacks heme a3, 10-15% contains heme a3 but lacks CuB. CuA assembly is unaffected
additional information
-
an assembled complex IV is required to maintain the stability of complex I in a mouse cell line with suppressed expression of subunit 4 of complex IV
additional information
-
CcO activity in cox19DLETA cells is less than 10% of wild-type levels
additional information
-
a strain lacking the Cox10 protein responsible for heme A synthesis, results in no expression of functional CytcO
additional information
-
CcO activity in cox19DLETA cells is less than 10% of wild-type levels
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2
20°C, 2 days, the enzyme retains about 30% residual activity
742013
3
20°C, 2 days, the enzyme retains about 42% residual activity
742013
4
20°C, 2 days, the enzyme retains about 65-60% residual activity
742013
6 - 10
20°C, 2 days, the enzyme retains about 70% residual activity
742013
5
-
irreversible denaturation below, protection by incorporation into proteoliposomes
396013
5
-
irreversible denaturation below, protection by incorporation into proteoliposomes
396013
5
20°C, 2 days, the enzyme retains about 65-60% residual activity
742013
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 61
-
the half-life of the enzyme at 37°C is 0.4 h, the dissociation of subunit III and/or VIIa is responsible for temperature-induced inactivation of the enzyme at 61°C
additional information
additional information
-
thermal denaturation in lipid phase consisting of 4 sequential melting steps, beginning with denaturation of subunit III
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM Tris-HCl buffer, pH 8.0, 0.5% Tween 20, several months, stable
-
0°C, 100 mM, potassium phosphate, pH 7.4, 0.5% Tween 20, 6 d, 40-50% loss of activity
-
20°C, 2 days, pH 6.0-10.0, the enzyme retains about 70% residual activity
4°C, 0.2 M phosphate buffer, 2% cholate, decrease of solubility during long term storage
-
liquid N2, 10 mM Tris-HCl buffer, pH 8.0, 0.5% Tween 20
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration
by small-scale immunopurification
carboxymethyl cellulose, affinity chromatography on thiopropyl-Sepharose, subunit VIIc
-
DEAE Toyopearl 650C column chromatography and IMAC column chromatography
-
DEAE-Toyopearl column chromatography and hydroxyapatite column chromatography
-
gel filtration, ammonium sulfate, ion-exchange, affinity chromatography on yeast cytochrome c-Sepharose
-
hydrophobic chromatography, affinity chromatography on horse cytochrome c
-
literature overview
method 1: cytochrome c affinity chromatography, ion-exchange, method 2: ammonium sulfate, anion exchange, gel filtration
-
Ni-NTA Sepharose column chromatography and Superdex G75 gel filtration
-
recombinant wild-type, D407A, D407C and D407N mutant enzyme, Ni2+-nitrilotriacetic acid affinity chromatography
-
sodium cholate, ammonium sulfate, dispersion in 0.5% Tween 80
Triton X-100, DEAE-cellulose, DEAE-toyopearl, hydroxyapatite, ammonium sulfate
-
wild-type of soluble CuA domain and its mutants W121Y, DELTAW121 and W121L, expressed in Escherichia coli
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNAs from both COX19-1 splice variants cloned in the sense and antisense orientations in plasmid pYPGE15, containing a constitutive phosphoglycerate kinase gene promoter and a CYC1 terminator. Expressed in a yeast cox19 null mutant
-
COX subunit Vb open reading frame ligated into the pcDNA3.1/V5-His TOPO-TA expression vector and transfected into TOP10 Escherichia coli. Overexpression in HeLa-20 cells
-
expressed in cloned embryos which derive from Danio rerio embryonic nuclei and Gobiocypris rarus enucleated eggs
-
for the preparation of transcripts the plasmid GC-BS-COXIV-3'-UTR is used
-
overexpression of wild-type, D407A, D407C and D407N mutant enzyme in Rhodobacter sphaeroides
-
overexpression of wild-type, E148Q, D195N, E157Q, D214N, D188Q/E189N, D151Q/E152N, W143F, W143A and Y144A/W145A in Rhodobacter sphaeroides
-
Production of cytochrome c oxidase deficient strains and ANR deficient strain.
recombinant Cox19 expressed in Escherichia coli BL21 (pLysS) as a fusion protein with an 8-residue C-terminal Strep-tag II extension
-
the soluble CuA domain of subunit II of cytochrome c oxidase is cloned for expression in Escherichia coli cells
-
wild-type of soluble CuA domain and its mutants W121Y, DELTAW121 and W121L are expressed in Escherichia coli BL21
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cbb3-Cox activity and expression are maximal under microaerobiosis
Q5GCA8; Q5GCA7; Q5GCA5; Q5GCA6
enzyme activity declines progressively with age between 10 and 47 days by 33%
-
exposure of mouse Hepa1-6 cells to 10-30 microM pyrroloquinoline quinone for 24-48 h results in increased cytochrome c oxidase activity
-
expression of gelsolin in APP/Ps1 mice increases mitochondrial complex IV activity
-
Leigh syndrome most frequent trigger is deficiency of cytochrome c oxidase caused by mutations in the SURF1 gene
-
mutated human superoxide dismutase, SOD1, decreases the Cytox activity, but not the protein content of the Cytox subunit II
-
purified actin and Hsp90 maintain RNA-binding ability and specificity, inhibiting the COXIV messenger translation
-
the activity of cytochrome c oxidase is enhanced many folds under diazotrophic growth condition
-
there is a significant age-dependent decline in the cytochrome c oxidase activity
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
proton pumping activity of cytochrome c oxidase reconstituted in phospholipid vesicles
-
reconstitution
reconstitution into phospholipid vesicles
reconstitution into phospholipid vesicles in the presence of hydrophobic poly(vinyl alkanoate) polymers
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
cytochrome c oxidase modified electrodes can be used to distinguish amino acid sequence variations in proteins such as cytochrome c. This has potential relevance as a diagnostic for disease states, characterization of electron transfer reactions of cytochrome c isolated from ischemic and control hearts
drug development
medicine
nutrition
-
in beef muscles psoas major, longissimus lumborum, superficial semimembranosus, deep semimembranosus, and semitendinosus, comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity. Colour stability among muscles is variable and metmyoglobin-reducing activity is more useful than total reducing activity for explaining the role of reducing activity in muscle-colour stability
additional information
drug development
-
possibility of nonspecific peroxidation of various substances catalyzed by cytochrome oxidase via the peroxidase mechanism, which may contribute to intracellular metabolism of biologically active drugs (under conditions of cardiotoxicity) and other compounds
drug development
-
tumor necrosis factor alpha-mediated CcO inhibition leads to tissue dysoxia, which suppresses aerobic ATP production and causes a shift to the glycolytic pathway. Kinases and phosphatases involved in reversible tumor necrosis factor alpha-mediated CcO phosphorylation may be promising targets for drug development because they act on an end point of cell signaling
drug development
-
tumor necrosis factor alpha-mediated CcO inhibition leads to tissue dysoxia, which suppresses aerobic ATP production and causes a shift to the glycolytic pathway. Kinases and phosphatases involved in reversible tumor necrosis factor alpha-mediated CcO phosphorylation may be promising targets for drug development because they act on an end point of cell signaling
drug development
-
tumor necrosis factor alpha-mediated CcO inhibition leads to tissue dysoxia, which suppresses aerobic ATP production and causes a shift to the glycolytic pathway. Kinases and phosphatases involved in reversible tumor necrosis factor alpha-mediated CcO phosphorylation may be promising targets for drug development because they act on an end point of cell signaling
-
medicine
-
at therapeutic concentrations used for asthma relief, theophylline causes inhibition of the lung enzyme and decreases cellular ATP levels, suggesting a mechanism for its clinical action
medicine
A122T, i.e. m.6267G>A is a recurrent missense mutation in mitochondrially encoded cytochrome oxidase I specifically associated with cancer
medicine
-
amyloid beta which is involved in Alzheimers disease, specifically inhibits cytochrome-c oxidase
medicine
-
enzyme isoform cytochrome oxifdase III interacts with hepatitis B virus X protein
medicine
-
in skeletal muscle and brain of patients with mutations in genes SCO2 or SURF1, cytochrome-c oxidase holoenzyme is reduced to 10-20%, and to 10-30% in heart, whereas liver contains normal levels of enzyme. Heart, brain, and skeletal muscle of patients contain accumulated levels of enzyme subcomplexes of different subunits, but lacking subunit COX2. SCO2 is presumably involved in formation of the CuA centre of the COX2 subunit, and the lack of the CuA centre may result in decreased stability of COX2
medicine
-
6W/Kg GSM 900MHz microwaves may affect brain metabolism and neuronal activity (cytochrome c oxidase activity) in rats
medicine
-
a single injection of exogenous cytochrome c 24 h post-cecal ligation and puncture repletes mitochondrial substrate levels for up to 72 h, restores myocardial COX activity, and significantly improves survival
medicine
-
CO histochemistry, which reflects neuronal activity, is altered at all levels of the auditory system in Relnrl-Orl mutants (with Orleans mutation, which selectively affects cell migration, cell orientation, and to a more limited extent, cell number in the brain tissue)
medicine
-
cytochrome oxidase deficiency is a result of heme deficiency that may be relevant to the demyelinating phenotype of the neurodegenerative disease Friedreich's ataxia. Heme-based stimulation of ironsulfur cluster biogenesis is a rational strategy for the neurodegenerative disease Friedreich's ataxia
medicine
-
cytochrome oxidase is a metabolic target of caffeine. Stimulation of Cox activity by caffeine via blockade of A2AR signaling may be an important mechanism underlying the therapeutic benefits of caffeine in Parkinsons disease
medicine
cytochrome oxidase is a metabolic target of caffeine. Stimulation of Cox activity by caffeine via blockade of A2AR signaling may be an important mechanism underlying the therapeutic benefits of caffeine in Parkinsons disease
medicine
-
evidence of secondary loss of electron transport chain function (loss of complex II-III activity) resulting from a primary electron transport chain deficiency (of complex IV), which provides a possible mechanism for the progressive nature of mitochondrial encephalomyopathies and why in some patients multiple patterns of electron transport chain deficiencies may be demonstrated
medicine
-
hypoxia synergises with NO from neuronal nitric oxide synthase to induce neuronal death via cytochrome oxidase inhibition causing neuronal depolarisation. Neuronal nitric oxide synthase activity sensitises the cells to hypoxic-inhibition of cytochrome oxidase
medicine
-
in HIV-associated dementia, cortical neurons demonstrate decreased respiration upon HIV-1 neurotoxin trans activator of transcription proteint treatment, consistent with inhibition of the enzyme
medicine
-
lack of energy after traumatic brain injury caused by inhibition of CcO may be an important aspect of trauma pathology
medicine
-
low prenatal Cu intake by dams is the determinant of CCO activity in cardiac mitochondria of 21-d-old offspring and may lead to the assembly of a less-than-fully active holoenzyme
medicine
-
myocardial CcOX impairment can underlie CO induced cardiac dysfunction
medicine
-
protein kinase C epsilon is activated by hypoxia, which results in the activation of the mitochondrial protein CytCOx, which can protect the lens from mitochondrial damage under naturally hypoxic conditions observed in this tissue
medicine
-
recovery of enhanced cytochrome-c oxidase activity may play a role in ischemic preconditioning protection
medicine
-
relationship between the allosteric ATP-inhibition and phosphorylation of CcO subunit I, which apparently occurs in living cells, but is lost under stress (e.g. hypoxic stress)
medicine
-
relationship between the allosteric ATP-inhibition and phosphorylation of CcO subunit I, which apparently occurs in living cells, but is lost under stress (e.g. hypoxic stress)
medicine
-
simultaneous decrease in 2-deoxyglucose uptake and increase in COI mRNA expression are difficult to reconcile with the current model of basal ganglia function and suggest that the mechanisms by which high-frequency stimulation of the subthalamic nucleus exerts its clinical benefits are more complex than a simple reversal of abnormal activity in the subthalamic nucleus and its targets
medicine
-
the cholinesterase and monoamine oxidase inhibitor ladostigil may have a beneficial effect on cognitive deficits in Alzheimer's disease patients that have a reduction in cortical COx activity and cholinergic hypofunction
medicine
-
mutations in various mitochondrial enzymes can result in Leigh syndrome, among them cytochrome c oxidase
medicine
-
the copper-enzyme cytochrome c oxidase has been indicated as a primary molecular target of mutant copper, zinc superoxide dismutase in familial amyotrophic lateral sclerosis
medicine
Mus musculus C57B6 / S129
-
cytochrome oxidase is a metabolic target of caffeine. Stimulation of Cox activity by caffeine via blockade of A2AR signaling may be an important mechanism underlying the therapeutic benefits of caffeine in Parkinsons disease
-
additional information
100% homology among cox1 sequences from morphotype 1 (females presenting caudal tips smooth without spines) and morphotype 2 (females presenting caudal tips smooth with spines) of Filaria martis collected from beech martens, thus indicating that the shape of female posterior edge may vary among specimens
additional information
-
100% homology among cox1 sequences from morphotype 1 (females presenting caudal tips smooth without spines) and morphotype 2 (females presenting caudal tips smooth with spines) of Filaria martis collected from beech martens, thus indicating that the shape of female posterior edge may vary among specimens
additional information
-
an assembled complex IV helps to maintain complex I (NADH-ubiquinone oxidoreductase) in mammalian cells
additional information
-
an assembled complex IV helps to maintain complex I (NADH-ubiquinone oxidoreductase) in mammalian cells
additional information
-
Arabidopsis thaliana COX19 genes encode functional homologues of the yeast metal chaperone. Smaller COX19-1 isoform, but not the larger one, is able to restore growth on non-fermentable carbon sources when expressed in a yeast cox19 null mutant. Induction by biotic and abiotic stress factors may indicate a relevant role of this protein in the biogenesis of cytochrome c oxidase to replace damaged forms of the enzyme. COX19 has additional functions besides its participation in COX assembly as, for example, metal transport, detoxification, or general protection against oxidative stress
additional information
-
counteracting relationship exists between the effects of withdrawal and 17beta-estradiol on the activity of COX in a subunit specific manner, which may not alter protein synthesis
additional information
-
cytochrome c oxidase is involved in mercury reduction in Acidithiobacillus ferrooxidans cells. Levels of mercury resistance in Acidithiobacillus ferrooxidans strains correspond well with the levels of mercury resistance of cytochrome c oxidase
additional information
-
inhibition of COX activity is rather caused by ischemia-induced modification of COX polypeptides than by inhibition of mitochondrial translation
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, variation within Amiota spp. is 21.8%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, variation within Amiota spp. is 21.8%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, variation within Amiota spp. is 21.8%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, with a variation within Phortica spp. of 1.6%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, with a variation within Phortica spp. of 1.6%
additional information
-
mean nucleotide variation within the Steganinae subfamily is 8.1%, with a variation within Phortica spp. of 1.6%
additional information
-
molecular phylogenic analysis based on COXI indicates Gobiocypris rarus belongs to Gobioninae. Comparison of DNA with cDNA shows that RNA editing phenomenon does not occur in the COXI of Gobiocypris rarus
additional information
-
permeabilization of the outer mitochondrial membrane during apoptosis functions not just to release cytochrome c but also to maintain it oxidized via cytochrome oxidase, thus maximizing caspase activation
additional information
-
prion protein may not be involved in regulation of cytochrome c oxidase
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves
additional information
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the monomeric form of Rhodobacter sphaeroides COX when reconstituted into a phospholipid bilayer is completely functionally active in its ability to perform electron transfer and proton pumping activities of the enzyme
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EXTERNAL LINKS (specific for EC-Number 7.1.1.9)
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Release 2023.1 (January 2023)
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