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Dissection and engineering of the Escherichia coli formate hydrogenlyase complex

Lookup NU author(s): Professor Tracy Palmer FRS FRSE FMedSciORCiD, Professor Frank SargentORCiD


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© 2015 Federation of European Biochemical Societies.The Escherichia coli formate hydrogenlyase (FHL) complex is produced under fermentative conditions and couples formate oxidation to hydrogen production. In this work, the architecture of FHL has been probed by analysing affinity-tagged complexes from various genetic backgrounds. In a successful attempt to stabilize the complex, a strain encoding a fusion between FdhF and HycB has been engineered and characterised. Finally, site-directed mutagenesis of the hycG gene was performed, which is predicted to encode a hydrogenase subunit important for regulating sensitivity to oxygen. This work helps to define the core components of FHL and provides solutions to improving the stability of the enzyme.

Publication metadata

Author(s): McDowall JS, Hjersing MC, Palmer T, Sargent F

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 2015

Volume: 589

Issue: 20

Pages: 3141-3147

Print publication date: 07/10/2015

Online publication date: 07/09/2015

Acceptance date: 28/08/2015

ISSN (print): 0014-5793

ISSN (electronic): 1873-3468

Publisher: Elsevier


DOI: 10.1016/j.febslet.2015.08.043

PubMed id: 26358294


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Funder referenceFunder name
(GrantsBB/H001190/1 andBB/I02008X/1 to F.S.).
T.P. is Royal Society‐Wolfson Research Merit Award holder