Soybean lipoxygenase-catalyzed oxidations by linoleic acid hydroperoxide: different reducing substrates and dehydrogenation of phenidone and BW 755C.
Phenidone is not a substrate for dioxygenation by soybean lipoxygenase-1 (L1) but reduces L1Fe(III) into L1Fe(II), as shown by EPR spectroscopy. L1 catalyzes the oxidation of phenidone by 13-HPOD, the hydroperoxide formed by dioxygenation of linoleic acid by L1, with formation of 4,5-dehydrophenidone. Two moles of 13-HPOD are used per mole of phenidone dehydrogenated. Other pyrazoline derivatives such as BW 755C, but also, in a more general manner, different compounds containing phenol, aniline, hydrazine, hydroxylamine or hydrazide functions act as reducing substrates for decomposition of 13-HPOD by L1.
D015772:4,5-Dihydro-1-(3-(trifluoromethyl)phenyl)-1H-pyrazol-3-amine; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D008041:Linoleic Acids / Q000378:metabolism*; D008054:Lipid Peroxides / Q000378:metabolism*; D008084:Lipoxygenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D011720:Pyrazoles / Q000378:metabolism*; D013025:Glycine max; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity
D008041:Linoleic Acids; D008054:Lipid Peroxides; D011720:Pyrazoles; C008285:linoleic acid hydroperoxide; D015772:4,5-Dihydro-1-(3-(trifluoromethyl)phenyl)-1H-pyrazol-3-amine; D008084:Lipoxygenase; C015429:phenidone