Expanding the substrates for a bacterial hydrogenlyase reaction

Ciaran Lamont, Ciaran Kelly, Constanze Pinske, Grant Buchanan, Tracy Palmer, Frank Sargent

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)
14 Downloads (Pure)


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.
Original languageEnglish
Pages (from-to)649-653
Number of pages5
Issue number5
Early online date1 May 2017
Publication statusPublished - 1 May 2017


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