Artificial metalloenzymes: (Strept)avidin as host for enantioselective hydrogenation by achiral biotinylated rhodium-diphosphine complexes
Artificial metalloenzymes: (Strept)avidin as host for enantioselective hydrogenation by achiral biotinylated rhodium-diphosphine complexes
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DOI：
10.1021/ja0476718
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发表时间：
2004-11-10
影响因子：
15
通讯作者：
Ward, TR
中科院分区：
文献类型：
--
作者：
Skander, M;Humbert, N;Ward, TR
我们报道了基于生物素化的铑-双膦络合物非共价掺入(Strept)亲和素作为宿主蛋白的人工金属酶的产生。化学发生优化程序使人们能够优化用于还原乙酰氨基丙烯酸的对映选择性(在链霉亲和素S112G中高达96%的ee(R)和在WT亲和素中高达80%的ee(S))。在中性pH条件下，测得典型的阳离子生物素化双膦催化剂前体与宿主蛋白的结合常数：亲和素的logK-a=7.7(pl=10.4)，链霉亲和素的logK-a=7.1(pl=6.4)。结果表明，在30℃、催化剂负载量为1%的条件下，对映体选择性还原反应的最佳操作条件为5bar。
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.