Cytochrome c oxidase subunit II
"COX2" redirects here. For the cyclooxygenase isoenzyme, see COX-2.
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Location of the MT-CO2 gene in the human mitochondrial genome. MT-CO2 is one of the three cytochrome c oxidase subunit mitochondrial genes (orange boxes).
| Cytochrome c oxidase subunit II, transmembrane domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Bacterial cytochrome c oxidase complex. Subunit II indicated by blue. | |||||||||
| Identifiers | |||||||||
| Symbol | COX2_TM | ||||||||
| Pfam | PF02790 | ||||||||
| InterPro | IPR011759 | ||||||||
| PROSITE | PDOC00075 | ||||||||
| SCOP | 1occ | ||||||||
| SUPERFAMILY | 1occ | ||||||||
| TCDB | 3.D.4 | ||||||||
| OPM superfamily | 4 | ||||||||
| OPM protein | 1v55 | ||||||||
| |||||||||
| Cytochrome C oxidase subunit II, periplasmic domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | COX2 | ||||||||
| Pfam | PF00116 | ||||||||
| InterPro | IPR002429 | ||||||||
| PROSITE | PDOC00075 | ||||||||
| SCOP | 1occ | ||||||||
| SUPERFAMILY | 1occ | ||||||||
| TCDB | 3.D.4 | ||||||||
| OPM superfamily | 4 | ||||||||
| OPM protein | 1v55 | ||||||||
| CDD | cd13912 | ||||||||
| |||||||||
Cytochrome c oxidase subunit 2, also known as cytochrome c oxidase polypeptide II, is a protein that in humans is encoded by the MT-CO2 gene.[3]
Cytochrome c oxidase subunit II, abbreviated COXII, COX2, COII, or MT-CO2, is the second subunit of cytochrome c oxidase.
Structure
Cytochrome c oxidase (EC 1.9.3.1)[4][5] is an oligomeric enzymatic complex which is a component of the respiratory chain and is involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane. The enzyme complex consists of 3-4 subunits (prokaryotes) to up to 13 polypeptides (mammals). In Leigh's disease, there may be an abnormality or deficiency of cytochrome oxidase.
Function
Subunit 2 (COII) transfers the electrons from cytochrome c to the catalytic subunit 1. It contains two adjacent transmembrane regions in its N-terminus and the major part of the protein is exposed to the periplasmic or to the mitochondrial intermembrane space, respectively. COII provides the substrate-binding site and contains a copper centre called Cu(A) (see InterPro: IPR001505), probably the primary acceptor in cytochrome c oxidase. An exception is the corresponding subunit of the cbb3-type oxidase which lacks the copper A redox-centre. Several bacterial COII have a C-terminal extension that contains a covalently bound haem c.
The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ "Entrez Gene: COX2 cytochrome c oxidase subunit II".
- ↑ Capaldi RA, Malatesta F, Darley-Usmar VM (Jul 1983). "Structure of cytochrome c oxidase". Biochimica et Biophysica Acta. 726 (2): 135–48. doi:10.1016/0304-4173(83)90003-4. PMID 6307356.
- ↑ García-Horsman JA, Barquera B, Rumbley J, Ma J, Gennis RB (Sep 1994). "The superfamily of heme-copper respiratory oxidases". Journal of Bacteriology. 176 (18): 5587–600. PMC 196760
. PMID 8083153.
Further reading
- Torroni A, Achilli A, Macaulay V, Richards M, Bandelt HJ (Jun 2006). "Harvesting the fruit of the human mtDNA tree". Trends in Genetics. 22 (6): 339–45. doi:10.1016/j.tig.2006.04.001. PMID 16678300.
- Barrell BG, Bankier AT, Drouin J (Nov 1979). "A different genetic code in human mitochondria". Nature. 282 (5735): 189–94. doi:10.1038/282189a0. PMID 226894.
- Bodenteich A, Mitchell LG, Polymeropoulos MH, Merril CR (May 1992). "Dinucleotide repeat in the human mitochondrial D-loop". Human Molecular Genetics. 1 (2): 140. doi:10.1093/hmg/1.2.140-a. PMID 1301157.
- Lu X, Walker T, MacManus JP, Seligy VL (Jul 1992). "Differentiation of HT-29 human colonic adenocarcinoma cells correlates with increased expression of mitochondrial RNA: effects of trehalose on cell growth and maturation". Cancer Research. 52 (13): 3718–25. PMID 1377597.
- Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E (Dec 1991). "Normal variants of human mitochondrial DNA and translation products: the building of a reference data base". Human Genetics. 88 (2): 139–45. doi:10.1007/bf00206061. PMID 1757091.
- Moraes CT, Andreetta F, Bonilla E, Shanske S, DiMauro S, Schon EA (Mar 1991). "Replication-competent human mitochondrial DNA lacking the heavy-strand promoter region". Molecular and Cellular Biology. 11 (3): 1631–7. PMC 369459. PMID 1996112.
- Power MD, Kiefer MC, Barr PJ, Reeves R (Aug 1989). "Nucleotide sequence of human mitochondrial cytochrome c oxidase II cDNA". Nucleic Acids Research. 17 (16): 6734. doi:10.1093/nar/17.16.6734. PMC 318375. PMID 2550900.
- Attardi G, Chomyn A, Doolittle RF, Mariottini P, Ragan CI (1987). "Seven unidentified reading frames of human mitochondrial DNA encode subunits of the respiratory chain NADH dehydrogenase". Cold Spring Harbor Symposia on Quantitative Biology. 51 (1): 103–14. doi:10.1101/sqb.1986.051.01.013. PMID 3472707.
- Chomyn A, Cleeter MW, Ragan CI, Riley M, Doolittle RF, Attardi G (Oct 1986). "URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit". Science. 234 (4776): 614–8. doi:10.1126/science.3764430. PMID 3764430.
- Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G (1985). "Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase". Nature. 314 (6012): 592–7. doi:10.1038/314592a0. PMID 3921850.
- Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG (Apr 1981). "Sequence and organization of the human mitochondrial genome". Nature. 290 (5806): 457–65. doi:10.1038/290457a0. PMID 7219534.
- Montoya J, Ojala D, Attardi G (Apr 1981). "Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs". Nature. 290 (5806): 465–70. doi:10.1038/290465a0. PMID 7219535.
- Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N (Jan 1995). "Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs". Proceedings of the National Academy of Sciences of the United States of America. 92 (2): 532–6. doi:10.1073/pnas.92.2.532. PMC 42775. PMID 7530363.
- Ruvolo M, Zehr S, von Dornum M, Pan D, Chang B, Lin J (Nov 1993). "Mitochondrial COII sequences and modern human origins". Molecular Biology and Evolution. 10 (6): 1115–35. PMID 8277847.
- Polyak K, Li Y, Zhu H, Lengauer C, Willson JK, Markowitz SD, Trush MA, Kinzler KW, Vogelstein B (Nov 1998). "Somatic mutations of the mitochondrial genome in human colorectal tumours". Nature Genetics. 20 (3): 291–3. doi:10.1038/3108. PMID 9806551.
- Kato MV (Mar 1999). "The mechanisms of death of an erythroleukemic cell line by p53: involvement of the microtubule and mitochondria". Leukemia & Lymphoma. 33 (1-2): 181–6. doi:10.3109/10428199909093740. PMID 10194136.
- Andrews RM, Kubacka I, Chinnery PF, Lightowlers RN, Turnbull DM, Howell N (Oct 1999). "Reanalysis and revision of the Cambridge reference sequence for human mitochondrial DNA". Nature Genetics. 23 (2): 147. doi:10.1038/13779. PMID 10508508.
- Ingman M, Kaessmann H, Pääbo S, Gyllensten U (Dec 2000). "Mitochondrial genome variation and the origin of modern humans". Nature. 408 (6813): 708–13. doi:10.1038/35047064. PMID 11130070.
- Finnilä S, Lehtonen MS, Majamaa K (Jun 2001). "Phylogenetic network for European mtDNA". American Journal of Human Genetics. 68 (6): 1475–84. doi:10.1086/320591. PMC 1226134. PMID 11349229.
- Maca-Meyer N, González AM, Larruga JM, Flores C, Cabrera VM (2003). "Major genomic mitochondrial lineages delineate early human expansions". BMC Genetics. 2: 13. doi:10.1186/1471-2156-2-13. PMC 55343. PMID 11553319.
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