NADPH oxidase of neutrophils forms superoxide anion but does not reduce cytochrome c and dichlorophenolindophenol.
Superoxide (O-2) production by partially purified NADPH oxidase from guinea pig neutrophils was markedly increased when the cells were activated by exposure to phorbol-myristate acetate. On the contrary, NADPH-dependent cytochrome c and 2,6-dichlorophenolindophenol (DCIP) reductase activities in preparations from resting and activated neutrophils were similar. The apparent Km values for NADH and NADPH of the reductase activities were different from those of the O-2 producing enzyme. The electron acceptors did not inhibit the oxygen consumption by NADPH oxidase in the presence of superoxide dismutase. Even in anaerobiosis the oxidase failed to reduce cytochrome c and DCIP. These results suggest that NAD(P)H-dependent dye reductase activities are not involved in the electron transport system responsible for the O-2 production by neutrophils.
D015086:2,6-Dichloroindophenol / Q000378:metabolism*; D000693:Anaerobiosis; D000818:Animals; D003574:Cytochrome c Group / Q000378:metabolism*; D006168:Guinea Pigs; D007215:Indophenol / Q000031:analogs & derivatives*; D007700:Kinetics; D009247:NADH, NADPH Oxidoreductases / Q000097:blood*; D019255:NADPH Oxidases; D009251:NADPH-Ferrihemoprotein Reductase / Q000097:blood; D009504:Neutrophils / Q000201:enzymology*; D010101:Oxygen Consumption; D011808:Quinone Reductases / Q000097:blood; D013481:Superoxides / Q000378:metabolism*; D014969:Xanthine Oxidase / Q000378:metabolism
D003574:Cytochrome c Group; D013481:Superoxides; D007215:Indophenol; D015086:2,6-Dichloroindophenol; D014969:Xanthine Oxidase; D009247:NADH, NADPH Oxidoreductases; D009251:NADPH-Ferrihemoprotein Reductase; D019255:NADPH Oxidases; D011808:Quinone Reductases; C033633:dichlorophenolindophenol reductase