Enantioselective oxidations of sulfides catalyzed by chloroperoxidase.
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.
Colonna
S
S
Dipartimento di Chimica Organica e Industriale, Università di Milano, Italy.
Gaggero
N
N
Manfredi
A
A
Casella
L
L
Gullotti
M
M
Carrea
G
G
Pasta
P
P
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
D013440:Sulfides; D013454:Sulfoxides; D006735:Horseradish Peroxidase; D002711:Chloride Peroxidase