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

DOI: 10.1042/BCJ20180053

Authors: Stephen E. Beaton (University of Oxford) , Rhiannon M. Evans (University of Oxford) , Alexander J. Finney (University of Dundee) , Ciaran M Lamont (University of Dundee) , Fraser A. Armstrong (University of Oxford) , Frank Sargent (University of Dundee) , Stephen B. Carr (Research Complex at Harwell)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemical Journal

State: Published (Approved)
Published: March 2018
Diamond Proposal Number(s): 12346

Abstract: 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 tightly-bound 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 high-resolution crystal structures of HybOC and, hence, a prediction of the quaternary structure of the HybOCAB complex.

Journal Keywords: hydrogenase; metalloenzyme; Escherichia coli; iron-sulphur protein; protein structure

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I03-Macromolecular Crystallography

Other Facilities: PETRA III

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