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Information on EC 7.1.1.9 - cytochrome-c oxidase and Organism(s) Thermus thermophilus and UniProt Accession Q5SJ79

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IUBMB Comments
An oligomeric membrane heme-Cu:O2 reductase-type enzyme that terminates the respiratory chains of aerobic and facultative aerobic organisms. The reduction of O2 to water is accompanied by the extrusion of four protons. The cytochrome-aa3 enzymes of mitochondria and many bacterial species are the most abundant group, but other variations, such as the bacterial cytochrome-cbb3 enzymes, also exist. All of the variants have a conserved catalytic core subunit (subunit I) that contains a low-spin heme (of a- or b-type), a binuclear metal centre composed of a high-spin heme iron (of a-, o-, or b-type heme, referred to as a3, o3 or b3 heme), and a Cu atom (CuB). Besides subunit I, the enzyme usually has at least two other core subunits: subunit II is the primary electron acceptor; subunit III usually does not contain any cofactors, but in the case of cbb3-type enzymes it is a diheme c-type cytochrome. While most bacterial enzymes consist of only 3--4 subunits, the mitochondrial enzyme is much more complex and contains 14 subunits.
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Thermus thermophilus
UNIPROT: Q5SJ79
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The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
cytochrome c oxidase, cytochrome oxidase, complex iv, cytochrome c oxidase subunit i, cytochrome c oxidase subunit 1, cytochrome aa3, cytochrome-c oxidase, coxii, cytochrome a3, cox ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ba3-type cytochrome c oxidase
-
caa3-type cytochrome c oxidase
-
cytochrome c oxidase
-
ba3 cytochrome c oxidase
-
-
ba3-type cytochrome c oxidase
-
caa3 cytochrome c oxidase
-
caa3-type cytochrome c oxidase
-
complex IV (mitochondrial electron transport)
-
-
-
-
COXVIAH
-
-
-
-
cytochrome a3
-
-
-
-
cytochrome aa3
-
-
-
-
cytochrome ba3
-
-
-
-
cytochrome bb3
-
-
-
-
cytochrome c oxidase
Cytochrome caa3
-
-
-
-
cytochrome cbb3
-
-
-
-
ferrocytochrome c oxidase
-
-
-
-
indophenol oxidase
-
-
-
-
indophenolase
-
-
-
-
oxidase, cytochrome
-
-
-
-
Warburg's respiratory enzyme
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ferrocytochrome-c:oxygen oxidoreductase
An oligomeric membrane heme-Cu:O2 reductase-type enzyme that terminates the respiratory chains of aerobic and facultative aerobic organisms. The reduction of O2 to water is accompanied by the extrusion of four protons. The cytochrome-aa3 enzymes of mitochondria and many bacterial species are the most abundant group, but other variations, such as the bacterial cytochrome-cbb3 enzymes, also exist. All of the variants have a conserved catalytic core subunit (subunit I) that contains a low-spin heme (of a- or b-type), a binuclear metal centre composed of a high-spin heme iron (of a-, o-, or b-type heme, referred to as a3, o3 or b3 heme), and a Cu atom (CuB). Besides subunit I, the enzyme usually has at least two other core subunits: subunit II is the primary electron acceptor; subunit III usually does not contain any cofactors, but in the case of cbb3-type enzymes it is a diheme c-type cytochrome. While most bacterial enzymes consist of only 3--4 subunits, the mitochondrial enzyme is much more complex and contains 14 subunits.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-16-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
show the reaction diagram
-
-
-
?
O2 + 4 cyt c(Fe2+) + 8 H+/in
2 H2O + 4 cyt c(Fe3+) + 4 H+/out
show the reaction diagram
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
show the reaction diagram
ferrocytochrome c + O2
ferricytochrome c + H2O
show the reaction diagram
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
show the reaction diagram
ferrocytochrome c552 + O2 + H+
ferricytochrome c552 + H2O
show the reaction diagram
-
-
-
-
r
N,N,N',N'-tetramethyl-4-phenylendiamine + O2 + H+
?
show the reaction diagram
-
-
-
-
?
reduced ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2 + H+
oxidized ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine + H2O
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
show the reaction diagram
-
-
-
?
ferricytochrome c + H2O
ferrocytochrome c + O2 + H+
show the reaction diagram
ferrocytochrome c + O2 + H+
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme a
Heme a3
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
contains copper
Cu2+
-
contains copper
Fe3+
-
contains iron
Mg2+
contains Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
azide
-
0.11 mM, 50% inhibition, 10 mM, complete inhibition
CN-
-
0.0013 mM, 50% inhibition, 1 mM, complete inhibition
phosphate
Tween 20
-
0.5%, 40% inhibition
Tween 80
-
0.5% 60% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Phospholipid
-
activation
Triton X-100
-
0.5%, 10% activation
additional information
-
no activation with phospholipids
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.074
ferrocytochrome c
0.002 - 0.018
ferrocytochrome c552
-
0.23
reduced ascorbate-N,N,N',N'-tetramethyl-1,4-phenylenediamine
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.88 - 53
ferrocytochrome c
9.78
ferrocytochrome c552
-
-
-
7.5 - 60
N,N,N',N'-tetramethyl-4-phenylendiamine
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
1 * 52000 + 1 * 37000 + 1 * 29000, SDS-PAGE
33000
34000
-
1 * 71000 + 1 * 34000, subunit I shows anomalous behaviour on SDS-PAGE, Ferguson plot
37000
-
1 * 52000 + 1 * 37000 + 1 * 29000, SDS-PAGE
52000
-
1 * 52000 + 1 * 37000 + 1 * 29000, SDS-PAGE
55000
71000
-
1 * 71000 + 1 * 34000, subunit I shows anomalous behaviour on SDS-PAGE, Ferguson plot
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
trimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospholipoprotein
-
approx. 0.012 mmol/mg protein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
10 min, 100% activity
80
-
10 min, 76% activity
additional information
-
not cold labile
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
literature overview
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution into phospholipid vesicles, enzyme acts as proton pump
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Poole, R.K.
Bacterial cytochrome oxidases. A structurally and functionally diverse group of electron-transfer proteins
Biochim. Biophys. Acta
726
205-243
1983
Bacillus cereus, Bacillus subtilis, Thermus thermophilus, Paracoccus denitrificans, Cereibacter sphaeroides, Bacillus sp. PS3
Manually annotated by BRENDA team
Ludwig, B.
Cytochrome c oxidase in prokaryotes
FEMS Microbiol. Rev.
46
41-56
1987
Bacillus subtilis, Bacteria, Thermus thermophilus, Paracoccus denitrificans, Nitrobacter winogradskyi, no activity in Escherichia coli, Rhodobacter capsulatus, Cereibacter sphaeroides, Starkeya novella, Bacillus sp. PS3, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Manually annotated by BRENDA team
Ludwig, B.
Heme aa3-type cytochrome c oxidases from bacteria
Biochim. Biophys. Acta
594
177-189
1980
Bacteria, Bos taurus, Thermus thermophilus, Paracoccus denitrificans, Nitrobacter winogradskyi, Starkeya novella, Bacillus sp. PS3
Manually annotated by BRENDA team
Buse, G.; Hensel, S.; Fee, J.A.
Evidence for cytochrome oxidase subunit I and a cytochrome c subunit II fused protein in the cytochrome c1aa3 of Thermus thermophilus. How old is cytochrome oxidase?
Eur. J. Biochem.
181
261-268
1989
Thermus thermophilus
Manually annotated by BRENDA team
Fee, J.A.; Kuila, D.; Mather, M.W.; Yoshida, T.
Respiratory proteins from extremely thermophilic, aerobic bacteria
Biochim. Biophys. Acta
853
153-185
1986
Thermus thermophilus, Bacillus sp. PS3
Manually annotated by BRENDA team
Hon-nami, K.; Oshima, T.
Purification and characterization of cytochrome c oxidase from Thermus thermophilus HB8
Biochemistry
23
454-460
1984
Thermus thermophilus
-
Manually annotated by BRENDA team
Fee, J.A.; Choc, M.G.; Findling, K.L.; Lorence, R.; Yoshida, T.
Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8
Proc. Natl. Acad. Sci. USA
77
147-151
1980
Thermus thermophilus
Manually annotated by BRENDA team
Hon-nami, K.; Oshima, T.
Cytochrome oxidase from an extreme thermophile. Thermus thermophilus HB8
Biochem. Biophys. Res. Commun.
92
1023-1029
1980
Thermus thermophilus
Manually annotated by BRENDA team
Radzi Noor, M.; Soulimane, T.
Bioenergetics at extreme temperature: Thermus thermophilus ba3- and caa3-type cytochrome c oxidases
Biochim. Biophys. Acta
1817
638-649
2012
Thermus thermophilus (Q5SJ79), Thermus thermophilus (Q5SJ80), Thermus thermophilus (Q72H23), Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q5SJ79), Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72H23), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SJ80)
Manually annotated by BRENDA team
Noor, M.R.; Soulimane, T.
Structure of caa3 cytochrome c oxidase - a nature-made enzyme-substrate complex
Biol. Chem.
394
579-591
2013
Thermus thermophilus (P98005)
Manually annotated by BRENDA team
Du, W.G.; Noodleman, L.
Density functional study for the bridged dinuclear center based on a high-resolution X-ray crystal structure of ba3 cytochrome c oxidase from Thermus thermophilus
Inorg. Chem.
52
14072-14088
2013
Thermus thermophilus
Manually annotated by BRENDA team
Koutsoupakis, C.; Soulimane, T.; Varotsis, C.
Discrete ligand binding and electron transfer properties of ba3-cytochrome c oxidase from Thermus thermophilus evolutionary adaption to low oxygen and high temperature environments
Acc. Chem. Res.
52
1380-1390
2019
Thermus thermophilus (Q5SJ79), Thermus thermophilus, Thermus thermophilus DSM 579 (Q5SJ79)
Manually annotated by BRENDA team