A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans. | Zendy

Bernd Ludwig | Zendy; G. Schatz | Zendy

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A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans.

Author(s) -

Bernd Ludwig,

G. Schatz

Publication year - 1980

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.77.1.196

Subject(s) - cytochrome c oxidase , paracoccus denitrificans , cytochrome c1 , electron transport complex iv , cytochrome c , coenzyme q – cytochrome c reductase , cytochrome c peroxidase , cytochrome , biochemistry , cytochrome b , oxidase test , protein subunit , oxidoreductase , chemistry , biology , enzyme , mitochondrion , mitochondrial dna , gene

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.

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