Artificial metalloenzymes: (Strept)avidin as host for enantioselective hydrogenation by achiral biotinylated rhodium-diphosphine complexes

被引：131

作者：

Skander, M ^{[1
]}

Humbert, N ^{[1
]}

Collot, J ^{[1
]}

Gradinaru, J ^{[1
]}

Klein, G ^{[1
]}

Loosli, A ^{[1
]}

Sauser, J ^{[1
]}

Zocchi, A ^{[1
]}

Gilardoni, F ^{[1
]}

Ward, TR ^{[1
]}

机构：

[1] Univ Neuchatel, Inst Chem, CH-2007 Neuchatel, Switzerland

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 44期

关键词：

D O I：

10.1021/ja0476718

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We report on the generation of artificial metalloenzymes based on the noncovalent incorporation of biotinylated rhodium-diphosphine complexes in (strept)avidin as host proteins. A chemogenetic optimization procedure allows one to optimize the enantioselectivity for the reduction of acetamidoacrylic acid (up to 96% ee (R) in streptavidin S112G and up to 80% ee (S) in WT avidin). The association constant between a prototypical cationic biotinylated rhodium-diphosphine catalyst precursor and the host proteins was determined at neutral pH: log K-a = 7.7 for avidin (pl = 10.4) and log K-a = 7.1 for streptavidin (pl = 6.4). It is shown that the optimal operating conditions for the enantioselective reduction are 5 bar at 30 degreesC with a 1% catalyst loading.

引用

页码：14411 / 14418

页数：8

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