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 biotechnology have allowed the rapid optimization of existing enzymes for enantioselective processes. However, the ex nihilo creation of catalytic activity from a noncatalytic protein s...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2008-06, Vol.130 (25), p.8085-8088
Main Authors: Pordea, Anca, Creus, Marc, Panek, Jaroslaw, Duboc, Carole, Mathis, Déborah, Novic, Marjana, Ward, Thomas R
Format: Article
Language:English
Subjects:
Binding Sites
Biotin - chemistry
Circular Dichroism
Enzyme Stability
Enzymes - chemistry
Magnetic Resonance Spectroscopy
Oxidation-Reduction
Oxidoreductases - chemistry
Stereoisomerism
Streptavidin - chemistry
Sulfhydryl Compounds - chemistry
Vanadates - chemistry
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Summary: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.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja8017219