Supramolecular Assembly of Artificial Metalloenzymes Based on the Dimeric Protein LmrR as Promiscuous Scaffold
Supramolecular Assembly of Artificial Metalloenzymes Based on the Dimeric Protein LmrR as Promiscuous Scaffold
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DOI：
10.1021/jacs.5b05790
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发表时间：
2015-08-12
影响因子：
15
通讯作者：
Roelfes, Gerard
中科院分区：
文献类型：
--
作者：
Bos, Jeffrey;Browne, Wesley R.;Roelfes, Gerard
过渡金属配合物与蛋白质支架的超分子锚定是构建人工异构酶的一种很有吸引力的方法，因为这是通过自组装方便地实现的。在这里，我们报道了一种新的超分子人工金属酶的设计，它利用转录因子乳球菌多药耐药调节因子(LmrR)中心疏水空腔的混杂作为平面配位络合物的通用结合部位，而平面配位络合物不提供特定的蛋白质结合作用。这种方法的成功体现在铜(II)催化的吲哚对映体选择性Friedel Craft烷基化反应中表现出的良好的对映选择性。
Supramolecular anchoring of transition metal complexes to a protein scaffold is an attractive approach to the construction of artificial rnetalloenzymes since this is conveniently achieved by self-assembly. Here, we report a novel design for supramolecular artificial metalloenzymes that exploits the promiscuity of the central hydrophobic cavity of the transcription factor Lactococcal multidrug resistance Regulator (LmrR) as a generic binding site for planar coordination complexes that do not provide specific protein binding interactions. The success of this approach is manifested in the excellent enantioselectivities that are achieved in the Cu(II) catalyzed enantioselective Friedel Crafts alkylation of indoles.