Cytochrome b reduction by hexaammineruthenium in mitochondria and submitochondrial particles. Evidence for heme b-562 localization at the M-side of the mitochondrial membrane.
In the presence of ascorbate, hexaamineruthenium mediates rapid reduction of cytochrome b-562 in submitochondrial particles but not in mitochondria. The reaction is observed in the combined presence of antimycin (or funiculosin) and myxothiazol, which implies direct interaction of Ru(NH3)2+6 with b cytochrome(s). We assume that contrary to previous conclusions (Case and Leigh (1976) Biochem. J., 160, 769-783) redox centre of at least one of the oxidized cytochromes b, most probably of b-562, is exposed to the M-aqueous phase.
D000818:Animals; D002417:Cattle; D010856:Columbidae; D003573:Cytochrome b Group / Q000032:analysis / Q000378:metabolism*; D029968:Escherichia coli Proteins; D006418:Heme / Q000032:analysis; D007425:Intracellular Membranes / Q000378:metabolism*; D007700:Kinetics; D008929:Mitochondria, Heart / Q000378:metabolism*; D010084:Oxidation-Reduction; D012428:Ruthenium / Q000378:metabolism*; D017975:Ruthenium Compounds; D013367:Submitochondrial Particles / Q000378:metabolism*
D003573:Cytochrome b Group; D029968:Escherichia coli Proteins; D017975:Ruthenium Compounds; C031584:hexammineruthenium; D006418:Heme; D012428:Ruthenium; C017850:cytochrome b562, E coli