[NiFe], [FeFe], and [Fe] hydrogenase models from isomers
[NiFe], [FeFe], and [Fe] hydrogenase models from isomers
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DOI：
10.1126/sciadv.aaz8181
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发表时间：
2020-06-01
期刊：
影响因子：
13.6
通讯作者：
Hayami, Shinya
中科院分区：
文献类型：
--
作者：
Ogo, Seiji;Kishima, Takahiro;Hayami, Shinya
氢酶(H(2)酶)的研究是必要的，因为它们对未来的氢能经济具有重要意义。这些酶分为三类：倾向于H-2氧化的[NiFe]H(2)酶；倾向于H-2进化的[FeFe]H(2)酶；以及催化H-转移的[Fe]H(2)酶。到目前为止，对这些酶的建模将它们视为不同的物种，考虑到天然分子的不同核心和配体集，这是可以理解的。在这里，我们利用X射线分析和核磁共振、红外、穆斯堡尔谱和电化学测量证明，这三种酶的催化性能都可以用同一NiFe络合物的三个异构体来模拟。
The study of hydrogenase enzymes (H(2)ases) is necessary because of their importance to a future hydrogen energy economy. These enzymes come in three distinct classes: [NiFe] H(2)ases, which have a propensity toward H-2 oxidation; [FeFe] H(2)ases, which have a propensity toward H-2 evolution; and [Fe] H(2)ases, which catalyze H- transfer. Modeling these enzymes has so far treated them as different species, which is understandable given the different cores and ligand sets of the natural molecules. Here, we demonstrate, using x-ray analysis and nuclear magnetic resonance, infrared, Mossbauer spectroscopies, and electrochemical measurement, that the catalytic properties of all three enzymes can be mimicked with only three isomers of the same NiFe complex.