Transition metals mediate enzymatic inactivation caused by favism-inducing agents.
Enzymatic activity of purified or membrane-bound acetylcholine esterase was lost when incubated aerobically in the presence of both favism-inducing agent (isouramil or divicine) and copper ions. The requirement for oxygen could be substituted by hydrogen peroxide. Chelating agents provided total protection to the proteins. The suggested mechanism of enzymatic inactivation is analogous to that suggested earlier for the effects of superoxide and ascorbate, and involves the site-specific formation of hydroxyl radicals in the metal-mediated Haber-Weiss reaction. These findings may be relevant to the understanding of the pathogenesis of favism.
D001205:Ascorbic Acid / Q000494:pharmacology; D001463:Barbiturates / Q000494:pharmacology*; D002800:Cholinesterase Inhibitors; D003300:Copper / Q000502:physiology*; D004578:Electron Spin Resonance Spectroscopy; D005236:Favism / Q000201:enzymology*; D006801:Humans; D066298:In Vitro Techniques; D010084:Oxidation-Reduction; D011744:Pyrimidinones / Q000494:pharmacology*
D001463:Barbiturates; D002800:Cholinesterase Inhibitors; D011744:Pyrimidinones; C026511:divicine; C032211:isouramil; D003300:Copper; D001205:Ascorbic Acid