Human carbonic anhydrase II as host protein for the creation of artificial metalloenzymes: the asymmetric transfer hydrogenation of imines

被引：60
|
作者：
Monnard, Fabien W. [1 ]
Nogueira, Elisa S. [1 ]
Heinisch, Tillmann [1 ,2 ]
Schirmer, Tilman [2 ]
Ward, Thomas R. [1 ]
机构：
[1] Univ Basel, Dept Chem, CH-4056 Basel, Switzerland
[2] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland
来源：
CHEMICAL SCIENCE | 2013年 / 4卷 / 08期
关键词：
CATALYSTS; BINDING; INHIBITORS; COMPLEXES; REDUCTION; DESIGN; METALLOPROTEINS; ANCHOR; SITE;
D O I：
10.1039/c3sc51065d
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
In the presence of human carbonic anhydrase II, aryl-sulfonamide-bearing IrCp* pianostool complexes catalyze the asymmetric transfer hydrogenation of imines. Critical cofactor-protein interactions revealed by the X-ray structure of [(eta(5)-Cp*)Ir(pico 4)CI] 9 subset of WT hCA II were genetically optimized to improve the catalytic performance of the artificial metalloenzyme (68% ee, k(cat)/K-M 6.11 x 10(-3) min(-1) mM(-1)).
引用
收藏
页码：3269 / 3274
页数：6
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