Premium
Asymmetric sulfoxidations mediated by α‐chymotrypsin
Author(s) -
Das Prasanta Kumar,
Caaveiro Jose M. M.,
Luque Susana,
Klibanov Alexander M.
Publication year - 2002
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.10187
Subject(s) - chemistry , chymotrypsin , stereoselectivity , enzyme , hydrolysis , sulfide , stereochemistry , alkyl , sulfoxide , aqueous solution , active site , aryl , combinatorial chemistry , organic chemistry , catalysis , trypsin
The oxidation of aryl alkyl sulfides with H 2 O 2 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. © 2002 Wiley Periodicals, Inc. Biotechnol Bioeng 78: 104–109, 2002; DOI 10.1002/bit.10187