NADPH-dependent electron transport chain in microsomes and lipid peroxidation catalyzed by metal ions.
Like iron ions copper ions are also able to stimulate the NADPH-dependent lipid peroxidation in rat liver microsomes. This effect is strongly dependent on the concentration of Cu2+ added. Initial concentrations of Cu2+ above 50 microM completely inhibit the formation of malonaldehyde. The activator and inhibitor functions may be interpreted by a simultaneous participation of Cu+ ions formed in the chain branching and termination reaction of the free radical lipid peroxidation process. Inhibition studies with pCMB and the His-reagent diethyl pyrocarbonate indicate an essential role of cysteine and histidine residues in the Cu+-NADPH-dependent lipid peroxidation process.
D000818:Animals; D002729:Chloromercuribenzoates / Q000494:pharmacology; D003300:Copper / Q000494:pharmacology; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D007501:Iron / Q000494:pharmacology; D007700:Kinetics; D008054:Lipid Peroxides / Q000378:metabolism*; D008297:Male; D008315:Malondialdehyde; D008862:Microsomes, Liver / Q000378:metabolism*; D009249:NADP / Q000378:metabolism*; D051381:Rats
D002729:Chloromercuribenzoates; D008054:Lipid Peroxides; D008315:Malondialdehyde; D009249:NADP; D003300:Copper; D003577:Cytochrome P-450 Enzyme System; D007501:Iron