Soybean lipoxygenase-catalyzed oxidations by linoleic acid hydroperoxide: Different reducing substrates and dehydrogenation of phenidone and BW 755C
| Autor: | B. Biatry, Daniel Mansuy, C. Cucurou, J.P. Battioni |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Lipid Peroxides
Chemical Phenomena Linoleic acid Lipoxygenase Biophysics 4 5-Dihydro-1-(3-(trifluoromethyl)phenyl)-1H-pyrazol-3-amine Phenidone Hydrazide Biochemistry Catalysis Substrate Specificity chemistry.chemical_compound Aniline Hydroxylamine Phenol Organic chemistry Dehydrogenation Molecular Biology Chromatography High Pressure Liquid biology Cell Biology Chemistry Linoleic Acids chemistry biology.protein Pyrazoles Spectrophotometry Ultraviolet Soybeans Oxidation-Reduction |
| Zdroj: | Biochemical and Biophysical Research Communications. 151:339-346 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(88)90599-2 |
| Popis: | Phenidone is not a substrate for dioxygenation by soybean lipoxygenase-1 (L1) but reduces L1 Fe(III) into L1 Fe(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. |
| Databáze: | OpenAIRE |
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