Journal
JOURNAL OF CHEMICAL THEORY AND COMPUTATION
Volume 6, Issue 11, Pages 3490-3502Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ct100319b
Keywords
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Funding
- Department of Energy, Office of Basic Energy Sciences, Division of Materials Sciences and Engineering [DE-FG02-06ER-46344]
- Office of Science of the U.S. Department of Energy [DE-AC02-05CH11231]
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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.
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