Adamson, Hope, Robinson, Martin, Wright, John J. et al. (7 more authors) (2017) Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site. Journal of the American Chemical Society. pp. 10677-10686. ISSN 1520-5126
Abstract
The redox chemistry of the electron entry/exit site in Escherichia coli hydrogenase-1 is shown to play a vital role in tuning biocatalysis. Inspired by nature, we generate a HyaA-R193L variant to disrupt a proposed Arg-His cation-π interaction in the secondary coordination sphere of the outermost, "distal", iron-sulfur cluster. This rewires the enzyme, enhancing the relative rate of H 2 production and the thermodynamic efficiency of H 2 oxidation catalysis. On the basis of Fourier transformed alternating current voltammetry measurements, we relate these changes in catalysis to a shift in the distal [Fe 4S 4] 2+/1+ redox potential, a previously experimentally inaccessible parameter. Thus, metalloenzyme chemistry is shown to be tuned by the second coordination sphere of an electron transfer site distant from the catalytic center.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 American Chemical Society. |
Keywords: | Amino Acids/chemistry,Electrons,Hydrogen/chemistry,Hydrogenase/chemistry,Oxidation-Reduction |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) The University of York > Faculty of Sciences (York) > Biology (York) |
Funding Information: | Funder Grant number THE ROYAL SOCIETY UNSPECIFIED |
Depositing User: | Pure (York) |
Date Deposited: | 15 Aug 2017 11:30 |
Last Modified: | 25 Mar 2025 00:08 |
Published Version: | https://doi.org/10.1021/jacs.7b03611 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1021/jacs.7b03611 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:120187 |
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