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 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.
Institute of Chemistry, University of Neuchâtel, Avenue Bellevaux 51, CP 158,2009 Neuchâtel, Switzerland.
Anca
A
Pordea
Marc
M
Creus
Jaroslaw
J
Panek
Carole
C
Duboc
Déborah
D
Mathis
Marjana
M
Novic
Thomas R
TR
Ward
D001665:Binding Sites; D001710:Biotin / Q000737:chemistry; D002942:Circular Dichroism; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry*; D013237:Stereoisomerism; D019809:Streptavidin / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D014638:Vanadates / Q000737:chemistry*
D004798:Enzymes; D013438:Sulfhydryl Compounds; D014638:Vanadates; D001710:Biotin; D019809:Streptavidin; D010088:Oxidoreductases