Ilina, Yulia, Lorent, Christian, Katz, Sagie et al. (5 more authors) (2019) X-ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases. Angewandte Chemie - International Edition. ISSN 1433-7851
Abstract
[NiFe] hydrogenases are complex model enzymes for the reversible cleavage of dihydrogen (H2). However, structural determinants of efficient H2 binding to their [NiFe] active site are not properly understood. Here, we present crystallographic and vibrational-spectroscopic insights into the unexplored structure of the H2-binding [NiFe] intermediate. Using an F420-reducing [NiFe]-hydrogenase from Methanosarcina barkeri as a model enzyme, we show that the protein backbone provides a strained chelating scaffold that tunes the [NiFe] active site for efficient H2 binding and conversion. The protein matrix also directs H2 diffusion to the [NiFe] site via two gas channels and allows the distribution of electrons between functional protomers through a subunit-bridging FeS cluster. Our findings emphasize the relevance of an atypical Ni coordination, thereby providing a blueprint for the design of bio-inspired H2-conversion catalysts.
Metadata
Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2019 The Authors. |
Keywords: | biocatalysis, crystal structure, hydrogen activation, vibrational spectroscopy, [NiFe] hydrogenase |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 18 Nov 2019 12:50 |
Last Modified: | 11 Feb 2024 00:35 |
Published Version: | https://doi.org/10.1002/anie.201908258 |
Status: | Published online |
Refereed: | Yes |
Identification Number: | https://doi.org/10.1002/anie.201908258 |
Related URLs: |
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