Issue 11, 2016

Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution

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.

Graphical abstract: Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution

Supplementary files

Article information

Article type
Edge Article
Submitted
09 Mar 2016
Accepted
29 Jun 2016
First published
11 Jul 2016
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2016,7, 6746-6752

Author version available

Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution

S. Katz, J. Noth, M. Horch, H. S. Shafaat, T. Happe, P. Hildebrandt and I. Zebger, Chem. Sci., 2016, 7, 6746 DOI: 10.1039/C6SC01098A

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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