Cytochrome c oxidase.
Within the past year, the structures of the cytochrome c oxidase from the soil bacterium Paracoccus denitrificans and of the metal centers of the cytochrome c oxidase from bovine heart mitochondria, both determined at 2.8 A resolution by X-ray crystallography, have been reported. The structures form a basis for understanding the mechanism of this redox-coupled transmembrane proton pump, which is the key component of the respiratory chain of most aerobic organisms.
Ostermeier
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Max-Planck-Institut für Biophysik, Abteilung für Molekulare Membranbiologie, Heinrich-Hoffmann-Strasse 7, 60528 Frankfurt, Germany. osti@argon.mpibp.uni-frankfurt.de
Iwata
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Michel
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D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000737:chemistry; D003576:Electron Transport Complex IV / Q000737:chemistry*; D008958:Models, Molecular; D010231:Paracoccus denitrificans / Q000201:enzymology*; D011487:Protein Conformation
D003300:Copper; D003576:Electron Transport Complex IV