Structural Basis for Enantioselectivity in the Transfer Hydrogenation of a Ketone Catalyzed by an Artificial Metalloenzyme

被引:19
作者
Cherrier, Mickal V. [1 ]
Engilberge, Sylvain [1 ]
Amara, Patricia [1 ]
Chevalley, Alice [2 ,3 ]
Salmain, Michele [2 ,3 ]
Fontecilla-Camps, Juan C. [1 ]
机构
[1] Univ Grenoble Alpes, Metalloprot Unit, Inst Biol Struct Jean Pierre Ebel, UMR 5075,CEA,CNRS, 41 Rue Horowitz, F-38027 Grenoble 1, France
[2] Chim ParisTech, Lab Charles Friedel, F-75005 Paris, France
[3] CNRS, UMR 7223, Paris, France
关键词
Metalloenzymes; Enantioselectivity; Structure elucidation; Proteins; Conformation analysis; BOVINE BETA-LACTOGLOBULIN; BIOTIN-AVIDIN TECHNOLOGY; BINDING SITE; FATTY-ACIDS; COMPLEXES; RUTHENIUM; LIPOCALIN; RHODIUM; DESIGN; HOST;
D O I
10.1002/ejic.201300592
中图分类号
O61 [无机化学];
学科分类号
070301 ; 081704 ;
摘要
The crystal structure of bovine -lactoglobulin bound to a complex consisting of a ((5)-Cp*)Rh(2,2-dipyridylamine) head and a lauric acid derived hydrophobic tail has been solved at 1.85 angstrom resolution. Previous work has shown that this hybrid catalyzes the transfer hydrogenation of an aryl ketone in neat water with formate as hydrogen donor with enantiomeric excess (ee) of about 26%. Calculations using the X-ray model indicate that the complex head can adopt discrete conformations, which may explain the ee observed.
引用
收藏
页码:3596 / 3600
页数:5
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