Lookup NU author(s): Professor Tracy Palmer,
Professor Frank Sargent
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
© 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.
Author(s): McDowall JS, Hjersing MC, Palmer T, Sargent F
Publication type: Article
Publication status: Published
Journal: FEBS Letters
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
PubMed id: 26358294
Altmetrics provided by Altmetric