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Involvement of cytochrome bc 1 complex and cytochrome c 2 in the electron‐transfer pathway for NO reduction in a photodenitrifier, Rhodobacter sphaeroides f.s. denitrificans
Author(s) -
Itoh Masahiko,
Mizukami Sally,
Matsuura Katsumi,
Satoh Toshio
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)81167-6
Subject(s) - rhodobacter sphaeroides , cytochrome , coenzyme q – cytochrome c reductase , chemistry , cytochrome c , electron transfer , cytochrome c1 , reductase , electron transport chain , cytochrome b6f complex , cytochrome p450 reductase , cytochrome c peroxidase , cytochrome b , antimycin a , stereochemistry , photochemistry , biochemistry , enzyme , mitochondrion , photosynthesis , mitochondrial dna , gene
The electron‐transfer pathway for NO reduction in a photodenitrifier, Rhodobacter sphaeroides f.s. denitrificans , was studied. A sample of membrane proteins containing cytochrome bc 1 complex and NO reductase activity was prepared from chromatophores using cholate/deoxycholate as detergents. The NO reductase activity was separated from the cytochrome bc 1 complex by ion‐exchange chromatography in the presence of dodecyl maltoside. When duroquinol was used as an electron donor, NO was reduced in the bc 1 ‐NO reductase preparation supplemented with cytochrome c 2 . The reduction was inhibited by antimycin and myxothiazol. These results indicate that the cytochrome bc 1 complex, cytochrome c 2 and membranous NO reductase are involved in the electron‐transfer pathway from quinol to NO in this photodenitrifier.