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Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance.

Naturally occurring oxygen tolerant NiFe membrane bound hydrogenases have a conserved catalytic bias towards hydrogen oxidation which limits their technological value. We present an Escherichia coli Hyd-1 amino acid exchange that apparently causes the catalytic rate of H2 production to double but do... Full description

Journal Title: Chemical communications (Cambridge England), July 12, 2016, Vol.52(58), pp.9133-9136
Main Author: Flanagan, Lindsey A
Other Authors: Wright, John J , Roessler, Maxie M , Moir, James W , Parkin, Alison
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1364-548X ; DOI: 1364-548X ; DOI: 10.1039/c6cc00515b
Link: http://search.proquest.com/docview/1803797146/?pq-origsite=primo
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recordid: proquest1803797146
title: Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance.
format: Article
creator:
  • Flanagan, Lindsey A
  • Wright, John J
  • Roessler, Maxie M
  • Moir, James W
  • Parkin, Alison
subjects:
  • Biocatalysis–Chemistry
  • Hydrogen–Metabolism
  • Hydrogenase–Metabolism
  • Oxidation-Reduction–Chemistry
  • Oxygen–Metabolism
  • Protein Engineering–Metabolism
  • Hydrogen
  • Nickel-Iron Hydrogenase
  • Hydrogenase
  • Oxygen
ispartof: Chemical communications (Cambridge, England), July 12, 2016, Vol.52(58), pp.9133-9136
description: Naturally occurring oxygen tolerant NiFe membrane bound hydrogenases have a conserved catalytic bias towards hydrogen oxidation which limits their technological value. We present an Escherichia coli Hyd-1 amino acid exchange that apparently causes the catalytic rate of H2 production to double but does not impact the O2 tolerance.
language: eng
source:
identifier: E-ISSN: 1364-548X ; DOI: 1364-548X ; DOI: 10.1039/c6cc00515b
fulltext: fulltext
issn:
  • 1364548X
  • 1364-548X
url: Link


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