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