Asymmetric sulfoxidations mediated by α-chymotrypsin

Das, Prasanta Kumar ; Caaveiro, Jose M. M. ; Luque, Susana ; Klibanov, Alexander M. (2002) Asymmetric sulfoxidations mediated by α-chymotrypsin Biotechnology and Bioengineering, 78 (1). pp. 104-109. ISSN 0006-3592

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The oxidation of aryl alkyl sulfides with H2O2 in aqueous solution is a reasonably facile reaction producing racemic sulfoxides. We show that in the presence of the hydrolytic enzyme α-chymotrypsin such a sulfoxidation is accelerated and, more importantly, becomes stereoselective. With phenyl isobutyl sulfide as a model, the chymotrypsin-mediated, highly asymmetric oxidation is shown to occur in the hydrophobic binding pocket of the enzyme active site. The stereoselectivity of the chymotrypsin-mediated sulfoxidations is correctly explained by means of structure-based molecular modeling of the enzyme-sulfide complexes.

Item Type:Article
Source:Copyright of this article belongs to John Wiley & Sons, Inc.
Keywords:Stereoselectivity; Sulfoxidation; Chymotrypsin; Molecular Modeling; Asymmetric Oxidation Sulfides
ID Code:108775
Deposited On:01 Feb 2018 11:24
Last Modified:01 Feb 2018 11:24

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