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Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site
[Image: see text] 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 o...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5562392/ https://www.ncbi.nlm.nih.gov/pubmed/28697596 http://dx.doi.org/10.1021/jacs.7b03611 |
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author | Adamson, Hope Robinson, Martin Wright, John J. Flanagan, Lindsey A. Walton, Julia Elton, Darrell Gavaghan, David J. Bond, Alan M. Roessler, Maxie M. Parkin, Alison |
author_facet | Adamson, Hope Robinson, Martin Wright, John J. Flanagan, Lindsey A. Walton, Julia Elton, Darrell Gavaghan, David J. Bond, Alan M. Roessler, Maxie M. Parkin, Alison |
author_sort | Adamson, Hope |
collection | PubMed |
description | [Image: see text] 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(4)S(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. |
format | Online Article Text |
id | pubmed-5562392 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-55623922017-08-21 Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site Adamson, Hope Robinson, Martin Wright, John J. Flanagan, Lindsey A. Walton, Julia Elton, Darrell Gavaghan, David J. Bond, Alan M. Roessler, Maxie M. Parkin, Alison J Am Chem Soc [Image: see text] 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(4)S(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. American Chemical Society 2017-07-12 2017-08-09 /pmc/articles/PMC5562392/ /pubmed/28697596 http://dx.doi.org/10.1021/jacs.7b03611 Text en Copyright © 2017 American Chemical Society This is an open access article published under a Creative Commons Attribution (CC-BY) License (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) , which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited. |
spellingShingle | Adamson, Hope Robinson, Martin Wright, John J. Flanagan, Lindsey A. Walton, Julia Elton, Darrell Gavaghan, David J. Bond, Alan M. Roessler, Maxie M. Parkin, Alison Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site |
title | Retuning
the Catalytic Bias and Overpotential of a
[NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron
Entry/Exit Site |
title_full | Retuning
the Catalytic Bias and Overpotential of a
[NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron
Entry/Exit Site |
title_fullStr | Retuning
the Catalytic Bias and Overpotential of a
[NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron
Entry/Exit Site |
title_full_unstemmed | Retuning
the Catalytic Bias and Overpotential of a
[NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron
Entry/Exit Site |
title_short | Retuning
the Catalytic Bias and Overpotential of a
[NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron
Entry/Exit Site |
title_sort | retuning
the catalytic bias and overpotential of a
[nife]-hydrogenase via a single amino acid exchange at the electron
entry/exit site |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5562392/ https://www.ncbi.nlm.nih.gov/pubmed/28697596 http://dx.doi.org/10.1021/jacs.7b03611 |
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