Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant H<sub>2</sub> supports its catalytic relevance-Reference-Cited by-同舟云学术

Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant H₂ supports its catalytic relevance

Published:2022 Issue:51 Volume:58 Page:7184-7187
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Senger Moritz¹^ORCID,Kernmayr Tobias²,Lorenzi Marco²^ORCID,Redman Holly J.²,Berggren Gustav²^ORCID

Affiliation:

1. Department of Chemistry, Physical Chemistry, Uppsala University, 75120 Uppsala, Sweden

2. Department of Chemistry, Molecular Biomimetics, Uppsala University, 75120 Uppsala, Sweden

Abstract

Studies of enzymatic catalysis often rely on non-biological reagents, which may affect catalytic intermediates and produce off-cycle states. Here the influence of buffer and reductant on key intermediates of [FeFe]-hydrogenase are explored.

Funder

H2020 European Research Council

H2020 Marie Skłodowska-Curie Actions

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CC/D2CC00671E

Reference49 articles.

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2. Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations

3. [FeFe]-Hydrogenases: recent developments and future perspectives

4. Molecular basis of [FeFe]-hydrogenase function

5. Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases

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