Cytochrome c oxidase
Encyclopedia : C : CY : CYT : Cytochrome c oxidase
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The enzyme cytochrome c oxidase (PDB [2OCC ], EC [1.9.3.1 ]) is a large transmembrane protein found in the mitochondrion and is the terminal electron acceptor in the electron transport chain (complex IV), taking 4 reducing equivalents from cytochrome c and converting molecular oxygen to water. In the process, it translocates protons, helping to establish a chemiosmotic potential that the ATP synthase then uses to synthesize ATP .
Summary reaction:
4 Fe2+ -cytochrome c + 4H+ + O2 → 4 Fe3+ -cytochrome c + 2 H2 O.
The complex is a large lipoprotein composed of several metal prosthetic sites and 13 protein subunits. In mammals, 10 subunits are nuclear in origin and 3 are synthesized mitochondrially. The complex contains 2 cytochrome s, the a and a3 cytochromes, and two copper centers, the CuA and CuB centers. In fact, the cytochrome a3 and CuB are a binuclear center that is the site of oxygen reduction. The mechanism of action of this large complex is still an active research topic.
Cyanide , carbon monoxide and azide all bind irreversibly to Cytochrome c Oxidase. The protein is then inhibited from functioning, causing chemical suffocation .
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