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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\u2010called \u2018complex\u2010I\u2010like\u2019 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\n                    <jats:italic>Pectobacterium atrosepticum<\/jats:italic>\n                    encoding formate hydrogenlyase-2 (FHL-2). A bank of\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    host strains, themselves devoid of various combinations of native formate hydrogenlyase genes, are employed to characterise FHL-2. We demonstrate that\n                    <jats:italic>P. atrosepticum<\/jats:italic>\n                    FHL-2 is active in an\n                    <jats:italic>E. coli<\/jats:italic>\n                    host in that it can generate H\n                    <jats:sub>2<\/jats:sub>\n                    under fermentative growth conditions. Unlike native\n                    <jats:italic>E. coli<\/jats:italic>\n                    formate hydrogenlyase-1 (FHL-1), recombinant\n                    <jats:italic>P. atrosepticum<\/jats:italic>\n                    FHL-2 cannot perform the reverse reaction and generate formic acid from H\n                    <jats:sub>2<\/jats:sub>\n                    and CO\n                    <jats:sub>2<\/jats:sub>\n                    . 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.\n                  <\/jats:p>","DOI":"10.1007\/s00775-026-02168-7","type":"journal-article","created":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T05:02:09Z","timestamp":1784782929000},"page":"521-535","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Genetic dissection of formate hydrogenlyase-2 function: a metalloenzyme involved in bacterial hydrogen production"],"prefix":"10.1007","volume":"31","author":[{"given":"Thomas C.P.","family":"Reed","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander J.","family":"Finney","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magali","family":"Roger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6841-3624","authenticated-orcid":false,"given":"Frank","family":"Sargent","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,7,23]]},"reference":[{"key":"2168_CR1","doi-asserted-by":"publisher","first-page":"11230","DOI":"10.1074\/jbc.M700728200","volume":"282","author":"JD Partridge","year":"2007","unstructured":"Partridge JD, Sanguinetti G, Dibden DP, Roberts RE, Poole RK et al (2007) Transition of Escherichia coli from aerobic to micro-aerobic conditions involves fast and slow reacting regulatory components. 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