HiPiP oxido-reductase activity in membranes from aerobically grown cells of the facultative phototroph Rhodoferax fermentans.
The role of the periplasmically located, water-soluble, HiPIP (high-potential iron-sulfur protein) in the respiratory chain of the facultative phototroph Rhodoferax fermentans has been examined. The oxidized HiPIP is reduced by succinate-dependent respiration via the bc1 complex, this reaction being inhibited by myxothiazol and/or stigmatellin. The reduced HiPIP can be oxidized by the membrane-bound cytochrome oxidase, this reaction being inhibited by 0.1 mM cyanide. We conclude that aerobically grown Rf. fermentans contains a redox chain in which HiPIP mediates electron transfer between the bc1 complex and the cb-type cytochrome oxidase.
D000332:Aerobiosis; D001426:Bacterial Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D004579:Electron Transport; D014450:Electron Transport Complex III / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010101:Oxygen Consumption; D045322:Photosynthetic Reaction Center Complex Proteins; D012244:Rhodospirillaceae / Q000254:growth & development / Q000378:metabolism*; D013053:Spectrophotometry
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; C007943:high potential iron-sulfur protein; D010088:Oxidoreductases; D003576:Electron Transport Complex IV; D014450:Electron Transport Complex III