Zipoli Federico, Car Roberto, Cohen Morrel H, Selloni Annabella
Department of Chemistry and Princeton Institute for the Science and Technology of Materials, Princeton University, Princeton, New Jersey 08544, and Department of Physics and Astronomy, Rutgers University, Piscataway, New Jersey 08854.
J Chem Theory Comput. 2010 Nov 9;6(11):3490-502. doi: 10.1021/ct100319b.
Bacterial di-iron hydrogenases produce hydrogen efficiently from water. Accordingly, we have studied by first-principles molecular-dynamics simulations (FPMD) electrocatalytic hydrogen production from acidified water by their common active site, the [FeFe]H cluster, extracted from the enzyme and linked directly to the (100) surface of a pyrite electrode. We found that the cluster could not be attached stably to the surface via a thiol link analogous to that which attaches it to the rest of the enzyme, despite the similarity of the (100) pyrite surface to the Fe4S4 cubane to which it is linked in the enzyme. We report here a systematic sequence of modifications of the structure and composition of the cluster devised to maintain the structural stability of the pyrite/cluster complex in water throughout its hydrogen production cycle, an example of the molecular design of a complex system by FPMD.
细菌双铁氢化酶能有效地从水中产生氢气。因此，我们通过第一性原理分子动力学模拟（FPMD）研究了从酶中提取并直接连接到黄铁矿电极（100）表面的常见活性位点[FeFe]H簇从酸化水中进行电催化产氢的过程。我们发现，尽管黄铁矿（100）表面与该簇在酶中连接的Fe4S4立方烷相似，但该簇无法通过类似于其与酶其余部分连接的硫醇键稳定地附着在表面上。我们在此报告了一系列对该簇结构和组成的系统性修饰，旨在在整个产氢循环中保持黄铁矿/簇复合物在水中的结构稳定性，这是一个通过FPMD对复杂系统进行分子设计的实例。
