MT-CO2
| Cytochrome c oxidase subunit II, transmembrane domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Bacterial complex. Subunit II indicated by blue.
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| Identifiers | |||||||||
| Symbol | COX2_TM | ||||||||
| Pfam | PF02790 | ||||||||
| InterPro | IPR011759 | ||||||||
| PROSITE | PDOC00075 | ||||||||
| SCOP | 1occ | ||||||||
| SUPERFAMILY | 1occ | ||||||||
| TCDB | 3.D.4 | ||||||||
| OPM superfamily | 4 | ||||||||
| OPM protein | 1v55 | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
| 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 | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
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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.
Cytochrome c oxidase subunit II, abbreviated COXII, COX2, COII, or MT-CO2, is the second subunit of .
(EC 1.9.3.1) 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.
Subunit 2 (COII) transfers the electrons from to the . 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.
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