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 optimization procedure allows one to produce (R)-acetamidoalanine with 96% enantioselectivity. These hybrid catalysts display features reminiscent both of enzymatic and of homogeneous systems.
Collot
Jérôme
J
Institute of Chemistry, University of Neuchâtel, Av. Bellevaux 51, CP 2, CH-2007 Neuchâtel, Switzerland.
Gradinaru
Julieta
J
Humbert
Nicolas
N
Skander
Myriem
M
Zocchi
Andrea
A
Ward
Thomas R
TR
D000179:Acrylates / Q000737:chemistry; D001360:Avidin / Q000737:chemistry*; D001710:Biotin / Q000737:chemistry*; D002384:Catalysis; D002934:Cinnamates / Q000737:chemistry; D004798:Enzymes / Q000737:chemistry*; D006865:Hydrogenation; D008667:Metalloproteins / Q000737:chemistry*; D012238:Rhodium / Q000737:chemistry*; D013237:Stereoisomerism; D019809:Streptavidin / Q000737:chemistry; D013379:Substrate Specificity
D000179:Acrylates; D002934:Cinnamates; D004798:Enzymes; D008667:Metalloproteins; D001360:Avidin; D001710:Biotin; D019809:Streptavidin; D012238:Rhodium