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InterPro: IPR000883 Cytochrome c oxidase, subunit I

Protein matchesHelp
UniProtKB
Matches:
99773 proteins
AccessionHelp IPR000883 Cyt_c_oxidase_su1
SecondaryHelp IPR002428
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR004677 Cytochrome c oxidase cbb3-type, subunit I
IPR014207 Cytochrome o ubiquinol oxidase, subunit I
IPR014233 Cytochrome aa3 quinol oxidase, subunit I
IPR014241 Cytochrome c oxidase, subunit I bacterial type
GO Term annotationHelp
Process GO:0009060 aerobic respiration
Function GO:0005506 iron ion binding
GO:0009055 electron carrier activity
GO:0020037 heme binding
Component GO:0016021 integral to membrane
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Cytochrome c oxidase (EC:1.9.3.1) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (EC:1.10.3), is directly involved in the coupling between dioxygen reduction and proton pumping [1, 2]. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes).

The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (CO I)) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members [3, 4, 5]. In contrast to eukaryotes the respiratory chain of prokaryotes is branched to multiple terminal oxidases. The enzyme complexes vary in haem and copper composition, substrate type and substrate affinity. The different respiratory oxidases allow the cells to customize their respiratory systems according to a variety of environmental growth conditions [1].

It has been shown that eubacterial quinol oxidase was derived from cytochrome c oxidase in Gram-positive bacteria and that archaebacterial quinol oxidase has an independent origin. A considerable amount of evidence suggests that proteobacteria (Purple bacteria) acquired quinol oxidase through a lateral gene transfer from Gram-positive bacteria [1].

Nitric oxide reductase (NOR) (EC:1.7.99.7) exists in denitrifying species of archae and eubacteria and is a heterodimer of cytochromes b and c. Phenazine methosulphate can act as acceptor. The prosite signature in this entry recognises the haem-copper site of the nitric oxidases.

Structural linksHelp
SCOP: f.24.1.1
CATH: 1.20.210.10
Database linksHelp
PDBe-motif: PS00077
Enzyme: EC:1.9.3.1
PROSITE doc: PDOC00074
PANDIT: PF00115
Blocks: IPB000883
COMe: PRX000181

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000883 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P00395 Cytochrome c oxidase subunit 1

P00397 Cytochrome c oxidase subunit 1

P00399 Cytochrome c oxidase subunit 1

P00401 Cytochrome c oxidase subunit 1

P24893 Cytochrome c oxidase subunit 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000883 Cytochrome c oxidase, subunit I
SWISS-MODEL
ModBase

PublicationsHelp
1. Garcia-Horsman JA, Barquera B, Rumbley J, Ma J, Gennis RB.
The superfamily of heme-copper respiratory oxidases.
J. Bacteriol. 176 5587-600 1994 [PubMed: 8083153]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=8083153
2. Papa S, Capitanio N, Glaser P, Villani G.
The proton pump of heme-copper oxidases.
Cell Biol. Int. 18 345-55 1994 [PubMed: 8049679]
http://dx.doi.org/10.1006/cbir.1994.1084
3. Castresana J, Lubben M, Saraste M, Higgins DG.
Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen.
EMBO J. 13 2516-25 1994 [PubMed: 8013452]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8013452
4. Capaldi RA, Malatesta F, Darley-Usmar VM.
Structure of cytochrome c oxidase.
Biochim. Biophys. Acta 726 135-48 1983 [PubMed: 6307356]
http://dx.doi.org/10.1016/0304-4173(83)90003-4
5. Holm L, Saraste M, Wikstrom M.
Structural models of the redox centres in cytochrome oxidase.
EMBO J. 6 2819-23 1987 [PubMed: 2824194]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=2824194&action=stream&blobtype=pdf

Additional ReadingHelp
Yoshikawa S, Shinzawa-Itoh K, Nakashima R, Yaono R, Yamashita E, Inoue N, Yao M, Fei MJ, Libeu CP, Mizushima T, Yamaguchi H, Tomizaki T, Tsukihara T.
Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase.
Science 280 1998 1723-9 [PubMed: 9624044]
http://dx.doi.org/10.1126/science.280.5370.1723
Qin L, Mills DA, Buhrow L, Hiser C, Ferguson-Miller S.
A conserved steroid binding site in cytochrome C oxidase.
Biochemistry 47 2008 9931-3 [PubMed: 18759498]
http://dx.doi.org/10.1021/bi8013483
Muramoto K, Hirata K, Shinzawa-Itoh K, Yoko-o S, Yamashita E, Aoyama H, Tsukihara T, Yoshikawa S.
A histidine residue acting as a controlling site for dioxygen reduction and proton pumping by cytochrome c oxidase.
Proc. Natl. Acad. Sci. U.S.A. 104 2007 7881-6 [PubMed: 17470809]
http://dx.doi.org/10.1073/pnas.0610031104
Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S.
The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A.
Science 272 1996 1136-44 [PubMed: 8638158]
http://www.sciencemag.org/cgi/content/abstract/272/5265/1136
Shinzawa-Itoh K, Aoyama H, Muramoto K, Terada H, Kurauchi T, Tadehara Y, Yamasaki A, Sugimura T, Kurono S, Tsujimoto K, Mizushima T, Yamashita E, Tsukihara T, Yoshikawa S.
Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase.
EMBO J. 26 2007 1713-25 [PubMed: 17332748]
http://dx.doi.org/10.1038/sj.emboj.7601618
Qin L, Hiser C, Mulichak A, Garavito RM, Ferguson-Miller S.
Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase.
Proc. Natl. Acad. Sci. U.S.A. 103 2006 16117-22 [PubMed: 17050688]
http://dx.doi.org/10.1073/pnas.0606149103
Saraste M, Castresana J.
Cytochrome oxidase evolved by tinkering with denitrification enzymes.
FEBS Lett. 341 1994 1-4 [PubMed: 8137905]
http://dx.doi.org/10.1016/0014-5793(94)80228-9
Hunsicker-Wang LM, Pacoma RL, Chen Y, Fee JA, Stout CD.
A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus.
Acta Crystallogr. D Biol. Crystallogr. 61 2005 340-3 [PubMed: 15735345]
http://dx.doi.org/10.1107/S0907444904033906
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InterPro 23.1