Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site

Hope Adamson; Martin Robinson; John J. Wright; Lindsey Anne Flanagan; Julia Walton; Darrell M Elton; David J Gavaghan; Alan M Bond; Maxie M. Roessler; Alison Parkin

doi:10.1021/jacs.7b03611

Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site

Hope Adamson, Martin Robinson, John J. Wright, Lindsey Anne Flanagan, Julia Walton, Darrell M Elton, David J Gavaghan, Alan M Bond, Maxie M. Roessler, Alison Parkin

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	10677-10686
Number of pages	10
Journal	Journal of the American Chemical Society
Volume	139
Issue number	31
Early online date	26 Jul 2017
DOIs	https://doi.org/10.1021/jacs.7b03611
Publication status	Published - 9 Aug 2017

Bibliographical note

Keywords

Amino Acids/chemistry
Catalysis
Electrons
Hydrogen/chemistry
Hydrogenase/chemistry
Oxidation-Reduction

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10.1021/jacs.7b03611

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Cite this

Adamson, H., Robinson, M., Wright, J. J., Flanagan, L. A., Walton, J., Elton, D. M., Gavaghan, D. J., Bond, A. M., Roessler, M. M., & Parkin, A. (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, 139(31), 10677-10686. https://doi.org/10.1021/jacs.7b03611

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title = "Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site",

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. ",

keywords = "Amino Acids/chemistry, Catalysis, Electrons, Hydrogen/chemistry, Hydrogenase/chemistry, Oxidation-Reduction",

author = "Hope Adamson and Martin Robinson and Wright, {John J.} and Flanagan, {Lindsey Anne} and Julia Walton and Elton, {Darrell M} and Gavaghan, {David J} and Bond, {Alan M} and Roessler, {Maxie M.} and Alison Parkin",

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Adamson, H, Robinson, M, Wright, JJ, Flanagan, LA, Walton, J, Elton, DM, Gavaghan, DJ, Bond, AM, Roessler, MM & Parkin, A 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, vol. 139, no. 31, pp. 10677-10686. https://doi.org/10.1021/jacs.7b03611

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T1 - Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site

AU - Adamson, Hope

AU - Robinson, Martin

AU - Wright, John J.

AU - Flanagan, Lindsey Anne

AU - Walton, Julia

AU - Elton, Darrell M

AU - Gavaghan, David J

AU - Bond, Alan M

AU - Roessler, Maxie M.

AU - Parkin, Alison

PY - 2017/8/9

Y1 - 2017/8/9

N2 - 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.

AB - 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.

KW - Amino Acids/chemistry

KW - Catalysis

KW - Electrons

KW - Hydrogen/chemistry

KW - Hydrogenase/chemistry

KW - Oxidation-Reduction

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DO - 10.1021/jacs.7b03611

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EP - 10686

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 31

ER -

Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site

Abstract

Bibliographical note

Keywords

Access to Document

Other files and links

Alison Parkin

Invited Talk at ACS meeting, New Orleans

Dr Alison Parkin/Professor Alan Bond International Exchanges Scheme

Dataset to support publication "Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site"

Cite this

Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site

Abstract

Bibliographical note

Keywords

Access to Document

Other files and links

Profiles

Alison Parkin

Activities

Invited Talk at ACS meeting, New Orleans

Projects

Dr Alison Parkin/Professor Alan Bond International Exchanges Scheme

Datasets

Dataset to support publication "Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site"

Cite this