A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans.
Cytochrome c oxidase (ferrocytochrome c: oxygen oxidoreductase, EC 1.9.3.1) was purified from the cytoplasmic membrane of the bacterium Paracoccus denitrificans. The enzyme contains two heme groups (a and a3) and two copper atoms per minimal unit, oxidizes mammalian cytochrome c at a high rate, and, when incorporated into liposomes, generates an electrochemical proton gradient during cytochrome c oxidation. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis reveals only two subunits of apparent molecular weights 45,000 and 28,000; they appear to correspond to the two largest mitochondrially made subunits of the seven-subunit cytochrome c oxidase isolated from yeast mitochondria. Because of its structural simplicity. Paracoccus cytochrome c oxidase offers new possibilities for exploring the mechanism of cytochrome c oxidase function.
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000378:metabolism; D008051:Lipid Bilayers; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology; D010231:Paracoccus denitrificans / Q000201:enzymology*; D014475:Uncoupling Agents / Q000494:pharmacology
D000596:Amino Acids; D001426:Bacterial Proteins; D008051:Lipid Bilayers; D046911:Macromolecular Substances; D014475:Uncoupling Agents; D003576:Electron Transport Complex IV