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

Author:

Senger Moritz1ORCID,Kernmayr Tobias2,Lorenzi Marco2ORCID,Redman Holly J.2,Berggren Gustav2ORCID

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

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