Artificial metalloenzyme for enantioselective sulfoxidation based on vanadyl-loaded streptavidin

Pordea, Anca and Creus, Marc and Panek, Jaroslaw and Duboc, Carole and Mathis, Deborah and Novic, Marjana and Ward, Thomas R.. (2008) Artificial metalloenzyme for enantioselective sulfoxidation based on vanadyl-loaded streptavidin. Journal of the American Chemical Society, 130 (25). pp. 8085-8088.

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Official URL: http://edoc.unibas.ch/dok/A5254471

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Nature’s catalysts are specifically evolved to carry out efficient and selective reactions. Recent developments in biotechnology 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 oxidation of prochiral sulfides with good enantioselectivities both for dialkyl and alkyl-aryl substrates (up to 93% enantiomeric excess). Electron paragmagnetic resonance spectroscopy, chemical 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.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Ward, Thomas R. R.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Chemical Society
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:24 Apr 2017 12:33
Deposited On:22 Mar 2012 14:06

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