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Expanding the substrates for a bacterial hydrogenlyase reaction

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



This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


© 2017 The Authors. Escherichia coli produces enzymes dedicated to hydrogen metabolism under anaerobic conditions. In particular, a formate hydrogenlyase (FHL) enzyme is responsible for the majority of hydrogen gas produced under fermentative conditions. FHL comprises a formate dehydrogenase (encoded by fdhF) linked directly to [NiFe]-hydrogenase-3 (Hyd-3), and formate is the only natural substrate known for proton reduction by this hydrogenase. In this work, the possibility of engineering an alternative electron donor for hydrogen production has been explored. Rational design and genetic engineering led to the construction of a fusion between Thermotoga maritima ferredoxin (Fd) and Hyd-3. The Fd-Hyd-3 fusion was found to evolve hydrogen when co-produced with T. maritima pyruvate:: ferredoxin oxidoreductase (PFOR), which links pyruvate oxidation to the reduction of ferredoxin. Analysis of the key organic acids produced during fermentation suggested that the PFOR/Fd- Hyd-3 fusion system successfully diverted pyruvate onto a new pathway towards hydrogen production.

Publication metadata

Author(s): Lamont CM, Kelly CL, Pinske C, Buchanan G, Palmer T, Sargent F

Publication type: Article

Publication status: Published

Journal: Microbiology

Year: 2017

Volume: 163

Issue: 5

Pages: 649-653

Print publication date: 01/05/2017

Online publication date: 10/04/2017

Acceptance date: 10/04/2017

Date deposited: 14/02/2019

ISSN (print): 1350-0872

ISSN (electronic): 1465-2080

Publisher: Microbiology Society


DOI: 10.1099/mic.0.000471


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