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二硫醇桥联镍铁配合物作为[NiFe]氢化酶活性位点的模型。

Dithiolato-bridged nickel-iron complexes as models for the active site of [NiFe]-hydrogenases.

作者信息

Song Li-Cheng, Yang Xi-Yue, Cao Meng, Gao Xiu-Yun, Liu Bei-Bei, Zhu Liang, Jiang Feng

机构信息

Department of Chemistry, State Key Laboratory of Elemento-Organic Chemistry, Nankai University, Tianjin 300071, China and Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Nankai University, Tianjin 300071, China.

Department of Chemistry, State Key Laboratory of Elemento-Organic Chemistry, Nankai University, Tianjin 300071, China.

出版信息

Chem Commun (Camb). 2017 Mar 30;53(27):3818-3821. doi: 10.1039/c7cc00149e.

DOI:10.1039/c7cc00149e
PMID:28287233
Abstract

The structural and functional modeling of the active site of [NiFe]-hydrogenases has been proved to be challenging to a great extent. Herein, we report the synthesis, structures, and some properties of the NiFe-based dicarbonyl, terminal hydride, and μ-hydroxo models for the active site of [NiFe]-hydrogenases.

摘要

[NiFe]氢化酶活性位点的结构和功能建模在很大程度上已被证明具有挑战性。在此,我们报道了用于[NiFe]氢化酶活性位点的镍铁基二羰基、端基氢化物和μ-羟基模型的合成、结构及一些性质。

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引用本文的文献

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Scaffold-based [Fe]-hydrogenase model: H activation initiates Fe(0)-hydride extrusion and non-biomimetic hydride transfer.基于支架的[铁]氢化酶模型:氢活化引发零价铁氢化物的挤出和非仿生氢化物转移。
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Bimetallic nickel-cobalt hydrides in H activation and catalytic proton reduction.
用于氢活化和催化质子还原的双金属镍钴氢化物。
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