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Cytochrome o ( bo ) is a proton pump in Paracoccus denitrificans and Escherichia coli
Author(s) -
Puustinen Anne,
Finel Moshe,
Virkki Marika,
Wikström Mårten
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80616-7
Subject(s) - paracoccus denitrificans , cytochrome , spheroplast , cytochrome c oxidase , coenzyme q – cytochrome c reductase , cytochrome c1 , cytochrome c , biochemistry , cytochrome b , chemistry , chemiosmosis , biology , escherichia coli , atp synthase , enzyme , mitochondrion , mitochondrial dna , gene
Spheroplasts from aerobically grown wild‐type Paracoccus denitrificans cells respire with succinate despite specific inhibition of the cytochrome bc 1 complex by myxothiazol. Coupled to this activity, which involves only b ‐type cytochromes, there is translocation of 1.5–1.9 H + /e − across the cytoplasmic membrane. Similar H + translocation ratios are observed during oxidation of ubiquinol in spheroplasts from aerobically grown mutants of Paracoccus lacking cytochrome c oxidase, or deficient in cytochrome c , as well as in a strain of E. coli from which cytochrome d was deleted. These observations show that the cytochrome o complex is a proton pump much like cytochrome aa 3 to which it is structurally related.