Asymmetric sulfoxidations mediated by α-chymotrypsin

Prasanta Kumar Das, Jose Manuel Martinez Caaveiro, Susana Luque, Alexander M. Klibanov

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)104-109
Number of pages6
JournalBiotechnology and Bioengineering
Volume78
Issue number1
DOIs
Publication statusPublished - Apr 5 2002
Externally publishedYes

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Chymotrypsin
Sulfides
Enzymes
Sulfoxides
Stereoselectivity
Oxidation
Molecular modeling
Molecular Structure
Catalytic Domain

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this

Asymmetric sulfoxidations mediated by α-chymotrypsin. / Das, Prasanta Kumar; Martinez Caaveiro, Jose Manuel; Luque, Susana; Klibanov, Alexander M.

In: Biotechnology and Bioengineering, Vol. 78, No. 1, 05.04.2002, p. 104-109.

Research output: Contribution to journalArticle

Das, Prasanta Kumar ; Martinez Caaveiro, Jose Manuel ; Luque, Susana ; Klibanov, Alexander M. / Asymmetric sulfoxidations mediated by α-chymotrypsin. In: Biotechnology and Bioengineering. 2002 ; Vol. 78, No. 1. pp. 104-109.
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