Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin−Avidin

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...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2003-07, Vol.125 (30), p.9030-9031
Main Authors: Collot, Jérôme, Gradinaru, Julieta, Humbert, Nicolas, Skander, Myriem, Zocchi, Andrea, Ward, Thomas R
Format: Article
Language:English
Subjects:
Acrylates - chemistry
Analytical, structural and metabolic biochemistry
Avidin - chemistry
Biological and medical sciences
Biotin - chemistry
Catalysis
Cinnamates - chemistry
Enzymes - chemistry
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrogenation
Metalloproteins - chemistry
Miscellaneous
Rhodium - chemistry
Stereoisomerism
Streptavidin - chemistry
Substrate Specificity
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Summary: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.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja035545i