Cox7a2 - cytochrome c oxidase subunit 7A2 (Norway rat)
Gene
Symbol
Taxonomy
Dates
- Create:2016-09-14
- Modify:2025-01-18
Description
Predicted to enable oxidoreductase activity. Predicted to be involved in mitochondrial respirasome assembly and regulation of oxidative phosphorylation. Predicted to be located in mitochondrial membrane. Predicted to be part of respiratory chain complex. Orthologous to several human genes including COX7A2 (cytochrome c oxidase subunit 7A2).
- Cox7a3
- cytochrome c oxidase subunit 7A2, mitochondrial
- cytochrome c oxidase polypeptide 7A2, mitochondrial
- cytochrome c oxidase polypeptide VIIa-liver/heart
- cytochrome c oxidase subunit VIIa 3
- cytochrome c oxidase subunit VIIa polypeptide 2
- cytochrome c oxidase subunit VIIa-L
- cytochrome c oxidase subunit VIIa-liver/heart
- cytochrome c oxidase, subunit 7a 3
- cytochrome c oxidase, subunit VIIa 2
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605
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