Superoxide dismutase inhibition of alkaline hemin-mediated O2 activation.
Inhibition of hemin-mediated O2 activation by bovine superoxide dismutase and the copper tetrammine complex has been examined. It is shown that the inhibitory effect of these species is not due to metabolism of O2-., but to a nonspecific inhibition of the process by the Cu2+ ion. We propose that the inhibition occurs at the level of electron transfer from NADH to iron in an analogous manner to that proposed for the Cu2+ inhibition of microsomal electron transfer.
Adams
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Department of Chemical Pathology, University of Cape Town Medical School, Republic of South Africa.
Adams
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D000818:Animals; D001711:Biotransformation / Q000187:drug effects; D002413:Cations, Divalent / Q000494:pharmacology; D002417:Cattle; D003300:Copper / Q000378:metabolism; D004837:Epinephrine / Q000378:metabolism; D004912:Erythrocytes / Q000201:enzymology; D006418:Heme / Q000031:analogs & derivatives*; D006427:Hemin / Q000037:antagonists & inhibitors*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D010084:Oxidation-Reduction; D010101:Oxygen Consumption / Q000187:drug effects*; D013482:Superoxide Dismutase / Q000494:pharmacology*; D015032:Zinc / Q000378:metabolism
D002413:Cations, Divalent; D006418:Heme; D006427:Hemin; D003300:Copper; D013482:Superoxide Dismutase; D015032:Zinc; D004837:Epinephrine