Dissection and engineering of the Escherichia coli formate hydrogenlyase complex

Jennifer S. McDowall; M. Charlotte Hjersing; Tracy Palmer; Frank Sargent

doi:10.1016/j.febslet.2015.08.043

Dissection and engineering of the Escherichia coli formate hydrogenlyase complex

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

Molecular Microbiology

Research output: Contribution to journal › Article › peer-review

21 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 language	English
Pages (from-to)	3141-3147
Number of pages	7
Journal	FEBS Letters
Volume	589
Issue number	20 Part B
DOIs	https://doi.org/10.1016/j.febslet.2015.08.043
Publication status	Published - 7 Oct 2015

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 7 Affordable and Clean Energy

Keywords

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

ASJC Scopus subject areas

Biochemistry
Biophysics
Cell Biology
Genetics
Molecular Biology
Structural Biology

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10.1016/j.febslet.2015.08.043

Cite this

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title = "Dissection and engineering of the Escherichia coli formate hydrogenlyase complex",

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.",

keywords = "Escherichia coli, Fermentation, Formate hydrogenlyase, Genetic engineering, Mutagenesis, [NiFe]-hydrogenase",

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year = "2015",

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AU - McDowall, Jennifer S.

AU - Hjersing, M. Charlotte

AU - Palmer, Tracy

AU - Sargent, Frank

PY - 2015/10/7

Y1 - 2015/10/7

N2 - 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.

AB - 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.

KW - Escherichia coli

KW - Fermentation

KW - Formate hydrogenlyase

KW - Genetic engineering

KW - Mutagenesis

KW - [NiFe]-hydrogenase

UR - https://www.scopus.com/pages/publications/84943197950

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DO - 10.1016/j.febslet.2015.08.043

M3 - Article

C2 - 26358294

AN - SCOPUS:84943197950

SN - 0014-5793

VL - 589

SP - 3141

EP - 3147

JO - FEBS Letters

JF - FEBS Letters

IS - 20 Part B

ER -

Dissection and engineering of the Escherichia coli formate hydrogenlyase complex

Abstract

UN SDGs

Keywords

ASJC Scopus subject areas

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