人工金属酶：（链）霉抗生物素蛋白作为宿主用于非手性生物素化铑-二膦配合物的对映选择性氢化反应
Artificial metalloenzymes: (strept)avidin as host for enantioselective hydrogenation by achiral biotinylated rhodium-diphosphine complexes.
作者信息
Skander Myriem, Humbert Nicolas, Collot Jérôme, Gradinaru Julieta, Klein Gérard, Loosli Andreas, Sauser Jérôme, Zocchi Andrea, Gilardoni François, Ward Thomas R
机构信息
Institute of Chemistry, University of Neuchâtel, Avenue Bellevaux 51, CP2, CH-2007 Neuchâtel, Switzerland.
出版信息
J Am Chem Soc. 2004 Nov 10;126(44):14411-8. doi: 10.1021/ja0476718.
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 (pI = 10.4) and log K(a) = 7.1 for streptavidin (pI = 6.4). It is shown that the optimal operating conditions for the enantioselective reduction are 5 bar at 30 degrees C with a 1% catalyst loading.
我们报道了基于生物素化铑二膦配合物在（链）霉抗生物素蛋白中作为宿主蛋白的非共价结合来生成人工金属酶。一种化学遗传优化程序能够优化对乙酰氨基丙烯酸还原反应的对映选择性（在链霉抗生物素蛋白S112G中高达96% ee（R），在野生型抗生物素蛋白中高达80% ee（S））。在中性pH下测定了典型阳离子生物素化铑二膦催化剂前体与宿主蛋白之间的缔合常数：抗生物素蛋白（pI = 10.4）的log K(a) = 7.7，链霉抗生物素蛋白（pI = 6.4）的log K(a) = 7.1。结果表明，对映选择性还原的最佳操作条件是在30℃、5巴压力下，催化剂负载量为1%。
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