Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases
Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases
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DOI：
10.1073/pnas.1204770109
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发表时间：
2012-07-17
影响因子：
11.1
通讯作者：
Armstrong, Fraser A.
中科院分区：
文献类型：
--
作者：
Hexter, Suzannah V.;Grey, Felix;Armstrong, Fraser A.
通过变温蛋白质膜伏安法和数学模型相结合的一系列实验，研究了含铁和含镍的酶催化快速有效的H+/H-2相互转化的非凡能力--这是铂金属独有的特性。这些结果突出了[FeFe]-氢酶和[NiFe]-氢酶的催化性能之间的重要差异，并证明了一个简单的酶和电催化剂中可逆催化电子流动的模型，该模型应该在电化学、催化和生物能量学等领域得到广泛应用。[FeFe]-氢酶的活性中心是一种复杂的铁-羰基复合体，被称为“H簇”，是一种最高的催化剂。
The extraordinary ability of Fe- and Ni-containing enzymes to catalyze rapid and efficient H+/H-2 interconversion-a property otherwise exclusive to platinum metals-has been investigated in a series of experiments combining variable-temperature protein film voltammetry with mathematical modeling. The results highlight important differences between the catalytic performance of [FeFe]-hydrogenases and [NiFe]-hydrogenases and justify a simple model for reversible catalytic electron flow in enzymes and electrocatalysts that should be widely applicable in fields as diverse as electrochemistry, catalysis, and bioenergetics. The active site of [FeFe]-hydrogenases, an intricate Fe-carbonyl complex known as the "H cluster," emerges as a supreme catalyst.