|Cytochrome C Oxidase is a vital part of almost every living creature. This metabolic protein catalyses the gerneration of a proton electrochemical gradient across the cell membrane (Ostermeier et al, 1996). It is divided into three subunits (I, II, II) in mammalian systems, but can be composed of up to 13 subunits in other systems (Ostermeier et al, 1996). Cytochrome C Oxidase Subunit II (COX) contains the binuclear CuA center, which transfers electrons from COX and transfers them to the oxygen-binding site. The Haem/copper terminal oxidases catalyse the reduction of dioxygen to water. Click here to see a rasmol image of mammalian Cytochrome C Oxydase Polypeptide II, and then compare it with the entire catalyst by Clicking Here.|
|Figure 1. This shows the catalytic cycle for Cytochrome
Figure complements of http://www-bioc.rice.edu/~graham/CcO.html
|To compare different forms of this protein you can click on the different hyperlinks available below all of them contain amino acid sequences and cDNA sequences.|
|Yeast (Saccharomyces cerevisiae)
Horse (Equus caballus)
Frog (Xenopus laevis)
Tarsius (Tarsius syrichta)
Cat (Felis catus)
1. Ostermeier, C., Iwata, S. and Michel, H.(1996) Cytochrome c oxidase. Curr. Opin. Struct. Biol. 6, 460-466.
2. Hill, B.C. (1994) Modeling the
sequence of electron transfer reactions in the single turnover of reduced,
mammalian cytochrome c oxidase with oxygen. J. Biol. Chem. 269, 2419-2425.
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