[Comparative study of effects of the tyrosine-copper(II) complex on xenobiotic hydroxylation and lipid peroxidation].
It has been found that NADPH-dependent hydroxylation of dimethylaniline, aniline, p- and o-nitroanisol and lipid peroxidation is inhibited by the tyrosine-copper (II) complex (low molecular weight analog of superoxide dismutase), which is indicative of a possibility of superoxide radicals formation in these reactions. The inhibition of the above-mentioned reactions with Tyr2-Cu2+ is less pronounced or absent, if cumole hydroperoxide is used as cosubstrate instead of NADPH. Differences in the Tyr2-Cu2+ complex effects on the cumule hydroperoxide-dependent xenobiotics hydroxylation and lipid peroxidation catalyzed by various forms of cytochrome P-450, e. g. microsomal, soluble and incorporated into liposomes, have been found. The data obtained suggest that the efficiency of the inhibitory effect of the Tyr2-Cu2+ complex depends on the type of cosubstrates (NADPH, cumole hydroperoxide) and substrates used as well as on the form of cytochrome P-450.
D000818:Animals; D003300:Copper / Q000494:pharmacology*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D007700:Kinetics; D008054:Lipid Peroxides / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000187:drug effects / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D009249:NADP; D010084:Oxidation-Reduction; D051381:Rats; D013482:Superoxide Dismutase; D013481:Superoxides; D014443:Tyrosine / Q000494:pharmacology*
D008054:Lipid Peroxides; D013481:Superoxides; D014443:Tyrosine; D009249:NADP; D003300:Copper; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D013482:Superoxide Dismutase
Sravnitel'noe issledovanie deĭtviia med'-tirozinobogo kompleksa na reaktsii gidroksilirovaniia ksenobiotikov i perekisnogo okisleniia lipidov.