The Structure of Hydrogenase-2 from Escherichia coli: Implications for H2 -Driven Proton Pumping

Stephen E. Beaton, Rhiannon M. Evans, Alexander J. Finney, Claire M. Lamont, Fraser A. Armstrong (Lead / Corresponding author), Frank Sargent (Lead / Corresponding author), Stephen B. Carr (Lead / Corresponding author)

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39 Citations (Scopus)
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Under anaerobic conditions Escherichia coli is able to metabolize molecular hydrogen via the action of several [NiFe]-hydrogenase enzymes. Hydrogenase-2, which is typically present in cells at low levels during anaerobic respiration, is a periplasmic-facing membrane-bound complex that functions as a proton pump to convert energy from H2 oxidation into a proton gradient; consequently, its structure is of great interest. Empirically, the complex consists of a tightlybound core catalytic module, comprising large (HybC) and small (HybO) subunits, which is attached to an Fe-S protein (HybA) and an integral membrane protein, HybB. To date, efforts to gain a more detailed picture have been thwarted by low native expression levels of hydrogenase-2 and the labile interaction between HybOC and HybA/HybB subunits. In this paper we describe a new over-expression system that has facilitated determination of highresolution crystal structures of HybOC and, hence, a prediction of the quaternary structure of the HybOCAB complex.
Original languageEnglish
Pages (from-to)1353-1370
Number of pages18
JournalBiochemical Journal
Issue number7
Early online date19 Mar 2018
Publication statusPublished - 16 Apr 2018


  • Hydrogenase
  • Metalloenzyme
  • Escherichia coli
  • Iron-sulphur protein
  • Protein structure

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Cell Biology


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