Abstract
This review deals with the mechanisms and stereochemistry of the enzymatic oxygenations of foreign organic sulfides promoted by two hepatic microsomal monooxygenases, i. e., cytochrome P-450 isolated from phenobarbital pretreated rabbit liver and pig liver microsomal FAD-containing monooxygenase (E. C. 1. 14. 13. 8). Oxygenation of sulfides with cytochrome P-450 procceds via a single electron transfer process from the substrate to the enzyme active site eventually affording both S-oxidation and S-dealkylation products, while FAD-containing monooxygenase catalyzes only the S-oxydation through electrophilic oxidation of divalent sulfur of the substrate by the peroxidic oxygen of the flavin-hydroperoxide intermediate. Stereochemistry of the sulfoxide formation is not highly controlled in the oxygenation of sulfides with cytochrome P-450, however, quite specific in the oxygenation of sulfides with FAD-monooxygenase.
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