Hydroperoxidase activity of lipoxygenase: hydrogen peroxide-dependent oxidation of xenobiotics.
Since H2O2 is one of the major biologically available peroxides, its ability to support hydroperoxidase activity of highly purified soybean lipoxygenase was examined by monitoring co-oxidation of selected xenobiotics. All of the eight chemicals tested were found to be oxidized in the presence of H2O2. Tetramethylbenzidine oxidation was completely inhibited by the classical lipoxygenase inhibitor nordihydroguaiaretic acid. The reaction was enzymatic in nature and exhibited a acidic pH optimum. The data clearly indicate, for the first time, that H2O2 can efficiently replace fatty acid hydroperoxide in a xenobiotic oxidation reaction medicated by the hydroperoxidase activity of lipoxygenase.
D001560:Benzidines / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008084:Lipoxygenase / Q000378:metabolism*; D009637:Masoprocol / Q000494:pharmacology; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D013379:Substrate Specificity
D001560:Benzidines; C020515:N,N,N',N'-tetramethylbenzidine; D009637:Masoprocol; D006861:Hydrogen Peroxide; D010544:Peroxidases; D008084:Lipoxygenase