Cytochrome c oxidase subunit I: Difference between revisions
m Journal cites:, added 1 Bibcode, using AWB (7751) |
→Human proteins containing this domain: trimmed list, all of the other entries were synonyms of MT-CO1 and many were pointed to erroneous pages |
||
| Line 38: | Line 38: | ||
*[[Cytochrome c oxidase, subunit I bacterial type]] {{InterPro|IPR014241}} |
*[[Cytochrome c oxidase, subunit I bacterial type]] {{InterPro|IPR014241}} |
||
== Examples == |
|||
==Human proteins containing this domain == |
|||
In humans, the main subunit of cytochrome c oxidase is encoded by the ''[[MT-CO1]]'' gene. |
|||
==References== |
==References== |
||
Revision as of 10:47, 20 July 2011
| Cytochrome C and Quinol oxidase polypeptide I | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 Structure of the 13-subunit oxidized cytochrome c oxidase.[1] | |||||||||||
| Identifiers | |||||||||||
| Symbol | COX1 | ||||||||||
| Pfam | PF00115 | ||||||||||
| InterPro | IPR000883 | ||||||||||
| PROSITE | PDOC00074 | ||||||||||
| SCOP2 | 1occ / SCOPe / SUPFAM | ||||||||||
| TCDB | 3.D.4 | ||||||||||
| OPM superfamily | 4 | ||||||||||
| OPM protein | 1v55 | ||||||||||
| |||||||||||
Cytochrome C and Quinol oxidase polypeptide I is main subunit of cytochrome c oxidase complex.
Cytochrome c oxidase (EC 1.9.3.1) is a key enzyme in aerobic metabolism. Proton pumping heme-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-heme a3 (or heme 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.[2][3] 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 heme-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin heme and copper B) as well as a low-spin heme, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.[4][5][6] In contrast to eukaryotes the respiratory chain of prokaryotes is branched to multiple terminal oxidases. The enzyme complexes vary in heme 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.[2]
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.[2]
A related nitric oxide reductase (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.
Subfamilies
- Cytochrome c oxidase cbb3-type, subunit I InterPro: IPR004677
- Cytochrome o ubiquinol oxidase, subunit I InterPro: IPR014207
- Cytochrome aa3 quinol oxidase, subunit I InterPro: IPR014233
- Cytochrome c oxidase, subunit I bacterial type InterPro: IPR014241
Examples
In humans, the main subunit of cytochrome c oxidase is encoded by the MT-CO1 gene.
References
- ^ Tsukihara T, Aoyama H, Yamashita E; et al. (1996). "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A". Science. 272 (5265): 1136–44. Bibcode:1996Sci...272.1136T. doi:10.1126/science.272.5265.1136. PMID 8638158.
{{cite journal}}: Explicit use of et al. in:|author=(help); Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ a b c Rumbley J, Gennis RB, Garcia-Horsman JA, Barquera B, Ma J (1994). "The superfamily of heme-copper respiratory oxidases". J. Bacteriol. 176 (18): 5587–5600. PMC 196760. PMID 8083153.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Glaser P, Villani G, Papa S, Capitanio N (1994). "The proton pump of heme-copper oxidases". Cell Biol. Int. 18 (5): 345–355. doi:10.1006/cbir.1994.1084. PMID 8049679.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Saraste M, Castresana J, Higgins DG, Lubben M (1994). "Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen". EMBO J. 13 (11): 2516–2525. PMC 395125. PMID 8013452.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Capaldi RA, Malatesta F, Darley-Usmar VM (1983). "Structure of cytochrome c oxidase". Biochim. Biophys. Acta. 726 (2): 135–48. PMID 6307356.
{{cite journal}}: Unknown parameter|unused_data=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Saraste M, Holm L, Wikstrom M (1987). "Structural models of the redox centres in cytochrome oxidase". EMBO J. 6 (9): 2819–2823. PMC 553708. PMID 2824194.
{{cite journal}}: CS1 maint: multiple names: authors list (link)