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

页码：3269 / 3274

页数：6

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