Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

New Approaches to an Old Problem: Original Techniques in [FeFe]-hydrogenase Research

Version 1 : Received: 11 April 2020 / Approved: 12 April 2020 / Online: 12 April 2020 (04:06:03 CEST)

How to cite: Land, H.; Senger, M.; Berggren, G.; Stripp, S.T. New Approaches to an Old Problem: Original Techniques in [FeFe]-hydrogenase Research. Preprints 2020, 2020040177 (doi: 10.20944/preprints202004.0177.v1). Land, H.; Senger, M.; Berggren, G.; Stripp, S.T. New Approaches to an Old Problem: Original Techniques in [FeFe]-hydrogenase Research. Preprints 2020, 2020040177 (doi: 10.20944/preprints202004.0177.v1).

Abstract

Even 20 years after the first crystal structures of [FeFe]-hydrogenase have been published, several aspects of biological hydrogen turnover are heatedly discussed. In this perspective, we give an overview on how the diversity of naturally occurring and artificially prepared, semi-synthetic [FeFe]-hydrogenases deepens our understanding of hydrogenase chemistry. In parallel, we cover new results from biophysical techniques that go beyond the scope of conventional electrochemistry, X-ray diffraction, EPR, and FTIR spectroscopy. Taking into account both proton transfer and electron transfer as well as the notorious sensitivity of [FeFe]-hydrogenases towards carbon monoxide, the discussion further touches upon the molecular proceedings of biological hydrogen turnover.

Subject Areas

hydrogen; biocatalysis; metalloenzymes; spectroscopy; biodiversity

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