 |
InterPro: IPR000883 Cytochrome c oxidase, subunit I
Protein matches
|
UniProtKB Matches: 99773 proteins |
|
Accession
|
IPR000883 Cyt_c_oxidase_su1 |
Secondary
|
IPR002428
|
Type
|
Family |
Signatures
|
|
InterPro Relationships
|
|
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 annotation
|
|
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
|
|
Entry Details in BioMart
|
Abstract
|
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 links
|
|
Database links
|
|
Publications
|
|
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 Reading
|
|
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
|
|
|
InterPro 23.1
|