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Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin−Avidin

Journal of the American Chemical SocietyPublished 1 July 2003
Jérôme Collot, Julieta Gradinaru, Nicolas Humbert, Myriem Skander, Andrea Zocchi, Thomas R. Ward
Citations252
SJR quartileQ1
SJR score5.55
SNIP2.61

TL;DR

A chemogenetic optimization procedure allows one to produce (R)-acetamidoalanine with 96% enantioselectivity and hybrid catalysts display features reminiscent both of enzymatic and of homogeneous systems.

Abstract

Homogeneous and enzymatic catalysis offer complementary means to generate enantiomerically pure compounds. Incorporation of achiral biotinylated rhodium-diphosphine complexes into (strept)avidin yields artificial metalloenzymes for the hydrogenation of N-protected dehydroamino acids. A chemogenetic optimization procedure allows one to produce (R)-acetamidoalanine with 96% enantioselectivity. These hybrid catalysts display features reminiscent both of enzymatic and of homogeneous systems.

Keywords

ChemistryBiochemistry, Genetics and Molecular Biology