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Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution
Citation key C6SC01098A
Author Katz, S. and Noth, J. and Horch, M. and Shafaat, H. S. and Happe, T. and Hildebrandt, P. and Zebger, I.
Pages 6746-6752
Year 2016
DOI 10.1039/C6SC01098A
Journal Chem. Sci.
Volume 7
Publisher The Royal Society of Chemistry
Abstract [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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