Combining acid-base, redox and substrate binding functionalities to give a complete model for the [FeFe]-hydrogenase

James M. Camara, Thomas B. Rauchfuss

Research output: Contribution to journalArticlepeer-review

Abstract

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(C 5 Me 4 CH 2 PEt 2) (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[(SCH 2) 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.

Original languageEnglish (US)
Pages (from-to)26-30
Number of pages5
JournalNature Chemistry
Volume4
Issue number1
DOIs
StatePublished - Jan 2012

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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