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...

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Veröffentlicht in:	Biochemistry (Easton) 1990-11, Vol.29 (46), p.10465-10468
Hauptverfasser:	Colonna, Stefano, Gaggero, N, Manfredi, A, Casella, L, Gullotti, M, Carrea, G, Pasta, P
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Biological and medical sciences Caldariomyces fumago Chloride Peroxidase - metabolism enzymatic activity Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Horseradish Peroxidase - metabolism Kinetics Marine Oxidation-Reduction Oxidoreductases redox reactions Stereoisomerism Substrate Specificity Sulfides - metabolism Sulfoxides - isolation & purification
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Beschreibung
Zusammenfassung:	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.
ISSN:	0006-2960 1520-4995
DOI:	10.1021/bi00498a006