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Soybean lipoxygenase-catalyzed oxidations by linoleic acid hydroperoxide: Different reducing substrates and dehydrogenation of phenidone and BW 755C

1988; Elsevier BV; Volume: 151; Issue: 1 Linguagem: Inglês

10.1016/0006-291x(88)90599-2

1090-2104

Daniel Mansuy, C. Cucurou, B. Biatry, J.‐P. BATTIONI,

Pharmacogenetics and Drug Metabolism

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.