NADPH-cytochrome-P-450 reductase promoted hydroxyl radical production by the iron(III)-ochratoxin A complex.
The Fe3+ complex of ochratoxin A has been shown to produce hydroxyl radicals in the presence of NADPH and NADPH-cytochrome-P-450 reductase. ESR spin-trapping experiments carried out in the presence of the hydroxyl radical scavenger ethanol and the spin trap DMPO (5,5-dimethyl-1-pyrroline-1-oxide) produced ESR spectra characteristic of the hydroxyl radial-derived carbon-centered DMPO-alkoxyl radical adduct. Thus hydroxyl radicals produced by the Fe3(+)-ochratoxin A complex in the presence of an enzymatic reductase may be be partly responsible for ochratoxin A toxicity.
Hasinoff
B B
BB
Department of Chemistry and Faculty of Medicine, Memorial University of Newfoundland, St. John's, Canada.
Rahimtula
A D
AD
Omar
R F
RF
D004578:Electron Spin Resonance Spectroscopy; D006878:Hydroxides; D017665:Hydroxyl Radical; D007501:Iron / Q000494:pharmacology*; D009251:NADPH-Ferrihemoprotein Reductase / Q000494:pharmacology*; D009793:Ochratoxins / Q000633:toxicity*; D013482:Superoxide Dismutase / Q000494:pharmacology
D006878:Hydroxides; D009793:Ochratoxins; C025589:ochratoxin A; D017665:Hydroxyl Radical; D007501:Iron; D013482:Superoxide Dismutase; D009251:NADPH-Ferrihemoprotein Reductase