Dissection and engineering of the Escherichia coli formate hydrogenlyase complex

Jennifer S. McDowall, M. Charlotte Hjersing, Tracy Palmer, Frank Sargent (Lead / Corresponding author)

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)3141-3147
Number of pages7
JournalFEBS Letters
Volume589
Issue number20 Part B
DOIs
Publication statusPublished - 7 Oct 2015

Keywords

  • Escherichia coli
  • Fermentation
  • Formate hydrogenlyase
  • Genetic engineering
  • Mutagenesis
  • [NiFe]-hydrogenase

Fingerprint Dive into the research topics of 'Dissection and engineering of the <i>Escherichia coli </i>formate hydrogenlyase complex'. Together they form a unique fingerprint.

  • Cite this