Rich, PR;
(2017)
Cytochrome c Oxidase: Insight into Functions from Studies of the Yeast S. cerevisiae Homologue.
In: Barber, J and Ruban, AV, (eds.)
Photosynthesis and Bioenergetics.
(pp. 65-80).
World Scientific Publishing: Singapore.
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Abstract
Different members of the superfamily of haem-copper oxidases have diverse substrates, cofactors and protein subunits. Nevertheless, all appear to catalyse oxygen reduction with a structurally-similar catalytic binuclear centre. This is housed in a common subunit I together with a low spin haem electron donor to the catalytic centre. All also appear to be coupled to additional proton translocation. However, the possible pathways for movement of protons through the protein structures are not universally conserved. Hence, although the basic mechanism of coupling is likely to follow similar principles, the detailed atomic mechanisms are likely to be different between the A and the B/C subgroups, and have even been suggested to differ between vertebrate mitochondrial cytochrome c oxidases and bacterial quinol and cytochrome c oxidases within the same A1 subgroup. Here, studies of the yeast mitochondrial homologue are reviewed that shed light on roles of different possible proton transfer pathways and some of the additional subunits found in mitochondrial enzymes.
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