Hydroperoxyflavin-mediated oxidations of organosulfur compounds. Model studies for the flavin monooxygenase.
Kinetic and product studies were carried out for the reaction of a synthetic hydroperoxyflavin with a series of organosulfur compounds as a model for the flavin-containing monooxygenase of mammalian liver (FMO). S-Oxidized products were identified, and the kinetics of the oxidation reactions were consistent with a mechanism involving attack of a sulfur nucleophile on the terminal oxygen atom of the hydroperoxyflavin. These results provide information about the substrate oxygenation step of FMO not available from steady-state enzyme kinetics.
D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases / Q000378:metabolism*; D005415:Flavins / Q000138:chemical synthesis* / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008954:Models, Biological; D010084:Oxidation-Reduction; D010545:Peroxides / Q000138:chemical synthesis* / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013431:Sulfates / Q000378:metabolism*
D005415:Flavins; D010545:Peroxides; D013431:Sulfates; C043035:4 alpha-hydroperoxy-5-ethyl-3,8,10-trimethylisoalloxazine; D001189:Aryl Hydrocarbon Hydroxylases