Structure and evolution of cytochrome oxidase.
The structural features of cytochrome oxidases are reviewed in light of their evolution. The substrate specificity (quinol vs. cytochrome c) is reflected in the presence of a unique copper centre (CuA) in cytochrome c oxidases. In several lines of evolution, quinol oxidases have independently lost this copper. Also, the most primitive cytochrome c oxidases do not contain this copper, and electron entry takes place via c-type haems. These enzymes, exemplified by the rhizobial FixN complex, probably remind the first oxidases. They are related to the denitrification enzyme nitric oxide reductase.
European Molecular Biology Laboratory, Heidelberg, Germany.
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D001419:Bacteria / Q000201:enzymology; D005075:Biological Evolution; D003300:Copper / Q000737:chemistry; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008954:Models, Biological; D015394:Molecular Structure; D010088:Oxidoreductases / Q000737:chemistry; D013379:Substrate Specificity
D003300:Copper; D010088:Oxidoreductases; C020094:duroquinol oxidase; C034747:nitric-oxide reductase; D003576:Electron Transport Complex IV