Enantioselective oxidations of sulfides catalyzed by chloroperoxidase
- 1 November 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (46) , 10465-10468
- https://doi.org/10.1021/bi00498a006
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.This publication has 15 references indexed in Scilit:
- An evidence of the peroxidase-dependent oxygen transfer from hydrogen peroxide to sulfidesBiochemical and Biophysical Research Communications, 1986
- Chemical reactivities of bleomycin.Journal of Biological Chemistry, 1985
- Asymmetric periodate oxidation of functionalized sulfides catalyzed by bovine serum albuminThe Journal of Organic Chemistry, 1985
- Analysis of the stable end products and intermediates of oxidative decarboxylation of indole-3-acetic acid by horseradish peroxidaseBiochemistry, 1984
- Functional differences between peroxidase compound I and the cytochrome P-450 reactive oxygen intermediate.Journal of Biological Chemistry, 1983
- Chloroperoxidase halogenation reactions. Chemical versus enzymic halogenating intermediates.Journal of Biological Chemistry, 1982
- Stereoselective oxidation of aromatic sulfides and sulfoxides in the binding domain of bovine serum albuminBioorganic Chemistry, 1981
- N-Demethylation reactions catalyzed by chloroperoxidase.Journal of Biological Chemistry, 1980
- ChloroperoxidaseJournal of Biological Chemistry, 1966
- CHLOROPEROXIDASE .2. ULTILIZATION OF HALOGEN ANIONS1966