[Comparative study of 1-naphthol oxidation by cytochrome P-450 and oxyhemoglobin].
The kinetics of 1-naphthol oxidation by rat liver microsomes in a phosphate buffer (pH 7.6) with participation of NADPH and O2 were studied at 9.5-27 degrees C. The activation energy of 1-naphthol oxidation (12.6 +/- 1.0 kcal/mol) was determined from the temperature dependence of initial oxidation rates. The kinetics of 1-naphthol oxidation by oxyhemoglobin in a phosphate buffer (pH 8.0) were studied at 13-25.5 degrees C. The activation energy equal to 17.7 +/- 1.0 kcal/mol for 1-naphthol oxidation by oxyhemoglobin was determined. The differences in oxidation mechanisms in the reactions with participation of cytochrome P-450 and oxyhemoglobin are discussed. Oxyhemoglobin Fe3+O2- interacts via one-electron way, whereas the microsomal cytochrome P-450 complex Fe3+O22- interacts with 1-naphthol via a two-electron way.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D007501:Iron; D007700:Kinetics; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism*; D009284:Naphthols / Q000378:metabolism*; D010084:Oxidation-Reduction; D010108:Oxyhemoglobins / Q000378:metabolism*; D051381:Rats
D009284:Naphthols; D010108:Oxyhemoglobins; D003577:Cytochrome P-450 Enzyme System; D007501:Iron
Sravńitel'noe izuchenie okisleniia 1-naftola s uchastiem tsitokhroma P-450 i oksigemoglobina.