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From the same journal

Re-tuning the Catalytic Bias and Overpotential of a [NiFe]-hydrogenase via a Single Amino Acid Exchange at the Electron Entry/exit Site

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Author(s)

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

Department/unit(s)

Publication details

JournalJournal of the American Chemical Society
DateAccepted/In press - 11 Jul 2017
DateE-pub ahead of print - 12 Jul 2017
DatePublished (current) - 9 Aug 2017
Issue number31
Volume139
Number of pages10
Pages (from-to)10677-10686
Early online date12/07/17
Original languageEnglish

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.

Bibliographical note

© 2017 American Chemical Society.

    Research areas

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

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