title: Enantioselective oxidations of sulfides catalyzed by chloroperoxidase.
abstract: The chloroperoxidase-catalyzed and horseradish peroxidase catalyzed oxidations of sulfides by tert-butyl and other peroxides have been investigated. The former metal enzyme afforded the corresponding sulfoxides having R absolute configuration in up to 92% enantiomeric excess (ee), whereas the latter gave racemic products. The various factors that control the enantioselectivity of the oxygenation have been examined.
authors: Dipartimento di Chimica Organica e Industriale, Università di Milano, Italy.
authors: S
authors: S
authors: Colonna
authors: N
authors: N
authors: Gaggero
authors: A
authors: A
authors: Manfredi
authors: L
authors: L
authors: Casella
authors: M
authors: M
authors: Gullotti
authors: G
authors: G
authors: Carrea
authors: P
authors: P
authors: Pasta
mesh_terms: D002711:Chloride Peroxidase / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D013237:Stereoisomerism; D013379:Substrate Specificity; D013440:Sulfides / Q000378:metabolism*; D013454:Sulfoxides / Q000302:isolation & purification
chemical_list: D013440:Sulfides; D013454:Sulfoxides; D006735:Horseradish Peroxidase; D002711:Chloride Peroxidase