Abstract
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.
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