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

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 output: Contribution to journalArticlepeer-review

    176 Citations (Scopus)

    Abstract

    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.
    Original languageEnglish
    Pages (from-to)3928-3938
    Number of pages11
    JournalJournal of Biological Chemistry
    Volume285
    Issue number6
    DOIs
    Publication statusPublished - 5 Feb 2010

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