Inorganic Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QR, United Kingdom.
Proc Natl Acad Sci U S A. 2012 Jul 17;109(29):11516-21. doi: 10.1073/pnas.1204770109. Epub 2012 Jul 16.
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.
一系列结合了变温蛋白膜伏安法和数学建模的实验研究了含铁和含镍酶将质子/氢气快速且高效地相互转化的非凡能力——这一特性在铂族金属之外是独一无二的。结果突出了[FeFe]-氢化酶和[NiFe]-氢化酶之间催化性能的重要差异，并为酶和电催化剂中可逆催化电子流提供了一个简单的模型，该模型应该在电化学、催化和生物能学等多个领域具有广泛的适用性。[FeFe]-氢化酶的活性中心是一种复杂的铁羰基复合物，称为“H 簇”，它是一种卓越的催化剂。
