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Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution

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  • S. Katz
  • J. Noth
  • M. Horch
  • H. S. Shafaat
  • T. Happe
  • P. Hildebrandt
  • I. Zebger


Publication details

JournalChemical Science
DateAccepted/In press - 29 Jun 2016
DatePublished (current) - 11 Jul 2016
Issue number11
Pages (from-to)6746-6752
Original languageEnglish


[FeFe] hydrogenases are biocatalytic model systems for the exploitation and investigation of catalytic hydrogen evolution. Here, we used vibrational spectroscopic techniques to characterize, in detail, redox transformations of the [FeFe] and [4Fe4S] sub-sites of the catalytic centre (H-cluster) in a monomeric [FeFe] hydrogenase. Through the application of low-temperature resonance Raman spectroscopy, we discovered a novel metastable intermediate that is characterized by an oxidized [FeIFeII] centre and a reduced [4Fe4S]1+ cluster. Based on this unusual configuration, this species is assigned to the first, deprotonated H-cluster intermediate of the [FeFe] hydrogenase catalytic cycle. Providing insights into the sequence of initial reaction steps, the identification of this species represents a key finding towards the mechanistic understanding of biological hydrogen evolution.

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