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Lookup NU author(s): Dr Tom ReedORCiD, Dr Alexander FinneyORCiD, Dr Magali Roger, Professor Frank SargentORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© The Author(s) 2026. Formate hydrogenlyases are metalloenzymes that can either produce molecular hydrogen gas or use H2 to convert carbon dioxide to formic acid, thus potentially contributing doubly to a sustainable energy future. The structure of formate hydrogenlyase reveals a membrane-bound redox enzyme that shares a common ancestor with the mitochondrial complex I (NADH dehydrogenase). As such, formate hydrogenlyase falls into a category of so‐called ‘complex‐I‐like’ enzymes, that are found in bacteria, archaea and eukaryotic organelles. They share a common core structure of a membrane arm (most likely involved in proton or ion translocation) and a peripheral arm containing metal cofactors and involved in electron transfer. In this work, we clone a gene cluster from Pectobacterium atrosepticum encoding formate hydrogenlyase-2 (FHL-2). A bank of Escherichia coli host strains, themselves devoid of various combinations of native formate hydrogenlyase genes, are employed to characterise FHL-2. We demonstrate that P. atrosepticum FHL-2 is active in an E. coli host in that it can generate H2 under fermentative growth conditions. Unlike native E. coli formate hydrogenlyase-1 (FHL-1), recombinant P. atrosepticum FHL-2 cannot perform the reverse reaction and generate formic acid from H2 and CO2. By testing different combinations of genes by taking an in vivo cross-complementation approach we conclude that the extended membrane arm exhibited by FHL-2 is a major factor in controlling directionality of the enzyme.
Author(s): Reed TCP, Finney AJ, Roger M, Sargent F
Publication type: Article
Publication status: Published
Journal: Journal of Biological Inorganic Chemistry
Year: 2026
Pages: Epub ahead of print
Online publication date: 23/07/2026
Acceptance date: 10/07/2026
Date deposited: 03/08/2026
ISSN (print): 0949-8257
ISSN (electronic): 1432-1327
Publisher: Springer Nature
URL: https://doi.org/10.1007/s00775-026-02168-7
DOI: 10.1007/s00775-026-02168-7
Data Access Statement: No datasets were generated or analysed during the current study.
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