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Proposal that the function of the membrane‐bound cytochrome a 1 ‐like haemoprotein (cytochrome b ‐595) in Escherichia coli is a direct electron donation to cytochrome d
Author(s) -
Poole Robert K.,
Williams Huw D.
Publication year - 1987
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(87)81240-1
Subject(s) - cytochrome , cytochrome b , cytochrome c1 , cytochrome c oxidase , coenzyme q – cytochrome c reductase , chemistry , hemeprotein , cytochrome p450 reductase , cytochrome c , cytochrome c peroxidase , heme , oxidase test , oxygen , biochemistry , photochemistry , enzyme , mitochondrion , organic chemistry , mitochondrial dna , gene
The cytochrome d ‐containing oxidase of oxygen‐limited Escherichia coli comprises cytochromes d , cytochrome b ‐558 and cytochrome b ‐595, previously called cytochrome a 1 . The reaction of the fully reduced complex with oxygen involves ligand binding to the ferrous haem d to form an oxygenated species, followed by oxidation of two b ‐type cytochromes, whose identity is unclear. Here we report kinetic studies on cytochrome b ‐595 oxidation and suggest that these results, together with optical and EPR data on the oxidase complex and its reaction with oxygen, are consistent with the hypothesis that the role of cytochrome b ‐595 is further reduction of the oxygen bound to cytochrome d .