Adamson, H, Robinson, M, Wright, JJ et al. (7 more authors) (2017) Re-tuning 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, 139 (31). pp. 10677-10686. ISSN 0002-7863
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 H₂ production and the thermodynamic efficiency of H₂ oxidation catalysis. On the basis of Fourier transformed alternating current voltammetry measurements, we relate these changes in catalysis to a shift in the distal [Fe₄S₄]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: | (c) 2017, The American Chemical Society. This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 06 Sep 2017 13:31 |
Last Modified: | 11 Sep 2017 13:08 |
Status: | Published |
Publisher: | American Chemical Society |
Identification Number: | 10.1021/jacs.7b03611 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:120887 |