Reduction of extracellular potassium ferricyanide by transmembrane NADH: (acceptor) oxidoreductase of human erythrocytes.
Reduction of extracellular ferricyanide by intact erythrocytes proceeds by a membrane bound, NADH-dependent reaction. It is depressed by a glycolysis inhibitor and a non penetrable sulfhydryl reagent, and activated by dehydroascorbate. Dehydroascorbate activation cannot be accounted for by release of reducing equivalents from the cells. It is concluded that the observed reaction is brought about by transmembrane NADH-acceptor oxidoreductase with donor binding at the inner and acceptor binding at the outer cell surface.
D003579:Cytochrome Reductases / Q000097:blood*; D003683:Dehydroascorbic Acid / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000201:enzymology*; D005292:Ferricyanides / Q000097:blood*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009245:NADH Dehydrogenase / Q000097:blood*; D010084:Oxidation-Reduction
D005292:Ferricyanides; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase; C028033:potassium ferricyanide; D003683:Dehydroascorbic Acid