Artificial Metalloenzyme for Enantioselective Sulfoxidation Based on Vanadyl-Loaded Streptavidin.

Nature's catalysts are specifically evolved to carry out efficient and selective reactions. Recent developments in biotechnol. have allowed the rapid optimization of existing enzymes for enantioselective processes. However, the ex nihilo creation of catalytic activity from a noncatalytic protein scaffold remains very challenging. Herein, we describe the creation of an artificial enzyme upon incorporation of a vanadyl ion into the biotin-binding pocket of streptavidin, a protein devoid of catalytic activity. The resulting artificial metalloenzyme catalyzes the enantioselective oxidn. of prochiral sulfides with good enantioselectivities both for dialkyl and alkyl-aryl substrates (up to 93{%} enantiomeric excess). ESR spectroscopy, chem. modification, and mutagenesis studies suggest that the vanadyl ion is located within the biotin-binding pocket and interacts only via second coordination sphere contacts with streptavidin. [on SciFinder(R)]

Références

Titre
Artificial Metalloenzyme for Enantioselective Sulfoxidation Based on Vanadyl-Loaded Streptavidin.
Type de publication
Article de revue
Année de publication
2008
Revue
J. Am. Chem. Soc.
Volume
130
Pagination
8085–8088
ISSN
0002-7863
Soumis le 12 avril 2018