Expanding the substrates for a bacterial hydrogenlyase reaction

Lamont, Ciaran M, Kelly, Ciarán, Pinske, Constanze, Buchanan, Grant, Palmer, Tracy and Sargent, Frank (2017) Expanding the substrates for a bacterial hydrogenlyase reaction. Microbiology, 163 (5). pp. 649-653. ISSN 1350-0872

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Official URL: https://doi.org/10.1099/mic.0.000471


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.

Item Type: Article
Uncontrolled Keywords: metabolic engineering, genetic engineering, fermentation, bio-hydrogen, hydrogenase, pyruvate :: ferredoxin oxidoreductase
Subjects: C700 Molecular Biology, Biophysics and Biochemistry
Department: Faculties > Health and Life Sciences > Applied Sciences
Depositing User: Paul Burns
Date Deposited: 26 Sep 2019 08:58
Last Modified: 31 Jul 2021 13:21
URI: http://nrl.northumbria.ac.uk/id/eprint/40861

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