Journal
NATURE CHEMISTRY
Volume 4, Issue 1, Pages 26-30Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nchem.1180
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- National Institutes of Health
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Some enzymes function by coupling substrate turnover with electron transfer from a redox cofactor such as ferredoxin. In the [FeFe]-hydrogenases, nature's fastest catalysts for the production and oxidation of H-2, the one-electron redox by a ferredoxin complements the one-electron redox by the diiron active site. In this Article, we replicate the function of the ferredoxins with the redox-active ligand Cp*Fe(C5Me4CH2PEt2) (FcP*). FcP* oxidizes at mild potentials, in contrast to most ferrocene-based ligands, which suggests that it might be a useful mimic of ferredoxin cofactors. The specific model is Fe-2[(SCH2)(2)NBn](CO)(3)(FcP*)(dppv) (1), which contains the three functional components of the active site: a reactive diiron centre, an amine as a proton relay and, for the first time, a one-electron redox module. By virtue of the synthetic redox cofactor, [1](2+) exhibits unique reactivity towards hydrogen and CO. In the presence of excess oxidant and base, H-2 oxidation by [1](2+) is catalytic.
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