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Cytochrome d
Cytochrome d is a protein that belongs to the Cytochrome family (electron-transporting proteins). Concretely, it is an enzyme – a protein that catalyses a chemical reaction. Cytochrome d is also known as cytochrome/heme a2. It is found in plenty of aerobic bacteria, especially when it has grown with a limited oxygen supply. The bacteria species in which it is more commonly found are Escherichia coli and Aerobacter aerogenes.〔(Cytochrome d group )〕
== General functions ==
Cytochrome d is, as other proteins of its family, a membrane-bound hemeprotein, but unlike cytochromes a and b, cytochrome D has a tetrapyrrolic chelate of iron as a prosthetic group instead of a heme A or heme B group. It is a dimeric protein, which means that is compound of two subunits (CydA〔(Caulobacter crescentus CB15 Enzyme: cytochrome d ubiquinol oxidase subunit I )〕 and CydB〔(Caulobacter crescentus CB15 Enzyme: cytochrome d ubiquinol oxidase subunit II )〕). At the same time, cytochrome d is part of the cytochrome bd-I terminal oxidase which catalyse the two electron oxidation of ubiquinol. This process is an oxidative phosphorylation that oxidizes the ubiquinol-8 to ubiquinone. The chemical reaction followed by this process is:
Ubiquinol-8 + O2 = Ubiquinone-8 + H2O〔(Cytochrome d ubiquinol oxidase subunit 1 )〕
By a similar reaction, it also catalyses the reduction of oxygen to water, which involves 4 electrons.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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