Discovery - University of Dundee - Online Publications

Library & Learning Centre

How Escherichia coli is equipped to oxidize hydrogen under different redox conditions

How Escherichia coli is equipped to oxidize hydrogen under different redox conditions

Research output: Contribution to journalArticle

View graph of relations


  • M.J. Lukey
  • A. Parkin
  • M.M. Roessler
  • B.J. Murphy
  • J. Harmer
  • F.A. Armstrong (Lead / Corresponding author)
  • T. Palmer
  • F. Sargent (Lead / Corresponding author)

Research units


Original languageEnglish
Pages (from-to)3928-3938
Number of pages11
JournalJournal of Biological Chemistry
Issue number6
StatePublished - 5 Feb 2010


The enterobacterium Escherichia coli synthesizes two H uptake enzymes, Hyd-1 and Hyd-2. We show using precise electrochemical kinetic measurements that the properties of Hyd-1 and Hyd-2 contrast strikingly, and may be individually optimized to function under distinct environmental conditions. Hyd-2 is well suited for fast and efficient catalysis in more reducing environments, to the extent that in vitro it behaves as a bidirectional hydrogenase. In contrast, Hyd-1 is active for H oxidation under more oxidizing conditions and cannot function in reverse. Importantly, Hyd-1 isO tolerant and can oxidize H in the presence of air, whereas Hyd-2 is ineffective for H oxidation under aerobic conditions. The results have direct relevance for physiological roles of Hyd-1 and Hyd-2, which are expressed in different phases of growth. The properties that we report suggest distinct technological applications of these contrasting enzymes. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

Research outputs



Library & Learning Centre

Contact | Accessibility | Policy