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 hydrogen (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 the present paper, we describe a new overexpression system that has facilitated the determination of high-resolution crystal structures of HybOC and, hence, a prediction of the quaternary structure of the HybOCAB complex.
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April 2018
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DAPI staining of Candida tropicalis cell chromatin, imaged by laser scanning confocal microscopy. In this issue of the Biochemical Journal, Li et al. discuss the potential to induce apoptosis when treating Candida tropicalis with CGA-N12; for details see pages 1385–1396.
Research Article|
April 16 2018
The structure of hydrogenase-2 from Escherichia coli: implications for H2-driven proton pumping
Stephen E. Beaton;
Stephen E. Beaton
1Department of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, Oxford OX1 3QR, U.K.
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Rhiannon M. Evans;
Rhiannon M. Evans
1Department of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, Oxford OX1 3QR, U.K.
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Alexander J. Finney;
Alexander J. Finney
2Division of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
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Ciaran M. Lamont;
Ciaran M. Lamont
2Division of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
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Fraser A. Armstrong
;
1Department of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, Oxford OX1 3QR, U.K.
Correspondence: Fraser A. Armstrong (fraser.armstrong@chem.ox.ac.uk) or Frank Sargent (f.sargent@dundee.ac.uk) or Stephen B. Carr (stephen.carr@rc-harwell.ac.uk)
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Frank Sargent
;
2Division of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
Correspondence: Fraser A. Armstrong (fraser.armstrong@chem.ox.ac.uk) or Frank Sargent (f.sargent@dundee.ac.uk) or Stephen B. Carr (stephen.carr@rc-harwell.ac.uk)
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Stephen B. Carr
3Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Oxford, Didcot OX11 0FA, U.K.
4Department of Biochemistry, University of Oxford, Oxford OX1 3QU, U.K.
Correspondence: Fraser A. Armstrong (fraser.armstrong@chem.ox.ac.uk) or Frank Sargent (f.sargent@dundee.ac.uk) or Stephen B. Carr (stephen.carr@rc-harwell.ac.uk)
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Publisher: Portland Press Ltd
Received:
January 19 2018
Revision Received:
March 12 2018
Accepted:
March 16 2018
Accepted Manuscript online:
March 19 2018
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2018
Biochem J (2018) 475 (7): 1353–1370.
Article history
Received:
January 19 2018
Revision Received:
March 12 2018
Accepted:
March 16 2018
Accepted Manuscript online:
March 19 2018
Citation
Stephen E. Beaton, Rhiannon M. Evans, Alexander J. Finney, Ciaran M. Lamont, Fraser A. Armstrong, Frank Sargent, Stephen B. Carr; The structure of hydrogenase-2 from Escherichia coli: implications for H2-driven proton pumping. Biochem J 16 April 2018; 475 (7): 1353–1370. doi: https://doi.org/10.1042/BCJ20180053
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