Bracing copper for the catalytic oxidation of C-H bonds
Bracing copper for the catalytic oxidation of C-H bonds
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DOI：
10.1038/s41929-018-0110-9
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发表时间：
2018-08-01
期刊：
影响因子：
37.8
通讯作者：
Walton, Paul H.
中科院分区：
文献类型：
--
作者：
Ciano, Luisa;Davies, Gideon J.;Walton, Paul H.
组氨酸支架是一些铜蛋白活性位点中发现的结构单元，由 N 端组氨酸组成，该组氨酸通过其氨基末端 NH2 和咪唑侧链的 pi-N 螯合单个铜离子。配位由另一个组氨酸侧链的 tau-N 完成，在铜离子处形成整体 N-3 T 形配位。组氨酸大括号出现在多种蛋白质中，包括裂解性多糖单加氧酶 LPMO 和颗粒甲烷单加氧酶 pMMO，两者都催化具有强 C-H 键（键解离焓 -100 kcal mol(-1)）的底物的氧化。因此，铜组氨酸支架是研究的重点，旨在了解自然如何催化未活化的 C-H 键的氧化。在本视角中，我们评估了这些研究，进一步为配位化学家设计和制备小分子铜氧化催化剂提供了受生物启发的方向。
A structural unit found in the active site of some copper proteins, the histidine brace, is comprised of an N-terminal histidine that chelates a single copper ion through its amino terminus NH2 and the pi-N of its imidazole side chain. Coordination is completed by the tau-N of a further histidine side chain, to give an overall N-3 T-shaped coordination at the copper ion. The histidine brace appears in several proteins, including lytic polysaccharide monooxygenases LPMOs and particulate methane monooxygenases pMMOs, both of which catalyse the oxidation of substrates with strong C-H bonds (bond dissociation enthalpies -100 kcal mol(-1)). As such, the copper histidine brace is the focus of research aimed at understanding how nature catalyses the oxidation of unactivated C-H bonds. In this Perspective, we evaluate these studies, which further give bioinspired direction to coordination chemists in the design and preparation of small molecule copper oxidation catalysts.