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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,10,27]]},"abstract":"<jats:p>\n                    The nitrogenase-like reductase CfbC\/D catalyzes the six-electron reduction of the tetrapyrrole macrocycle of Ni\n                    <jats:sup>2+<\/jats:sup>\n                    -sirohydrochlorin\n                    <jats:italic toggle=\"yes\">a,c<\/jats:italic>\n                    -diamide during the biosynthesis of coenzyme F\n                    <jats:sub>430<\/jats:sub>\n                    , an essential cofactor for biological methane formation and consumption. The individual dimeric protein components, CfbC\n                    <jats:sub>2<\/jats:sub>\n                    and CfbD\n                    <jats:sub>2<\/jats:sub>\n                    , form a complex to allow for electron transfer from the [4Fe:4S] cluster in CfbC\n                    <jats:sub>2<\/jats:sub>\n                    to the [4Fe:4S] cluster in CfbD\n                    <jats:sub>2<\/jats:sub>\n                    and onto the substrate. The overall process is ATP-dependent. Although CfbC\/D belongs to the family of nitrogenase-like enzymes, there are several intriguing differences between CfbC\/D, other nitrogenase-like enzymes and nitrogenase itself. In contrast to the other enzymes, CfbC\/D exhibits a simpler molecular architecture, forming a heterotetrameric CfbC\n                    <jats:sub>2<\/jats:sub>\n                    D\n                    <jats:sub>2<\/jats:sub>\n                    assembly. Furthermore, the interaction of the CfbC and CfbD components does not depend on the presence of adenosine triphosphate (ATP). Here we report cryoelectron microscopy structures of the CfbC\/D complex prepared in the absence and presence of substrates. These structures not only shed light on the molecular architecture of the CfbC\/D complex but also reveal a high degree of structural flexibility within the CfbD\n                    <jats:sub>2<\/jats:sub>\n                    component, which undergoes a large conformational change in the presence of an ATP analog and the tetrapyrrole substrate. The interplay of CfbD with its reductase CfbC also strongly suggests an evolutionary pathway toward the modern nitrogenase from methanogenic archaea.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2611794123","type":"journal-article","created":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T18:01:52Z","timestamp":1792519312000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":0,"title":["Conformational flexibility of the nitrogenase-like reductase CfbC\/D involved in coenzyme F\n                    <sub>430<\/sub>\n                    biosynthesis"],"prefix":"10.1073","volume":"123","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5431-5006","authenticated-orcid":false,"given":"Lin","family":"Zhang","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0245cg223","id-type":"ROR","asserted-by":"publisher"}],"name":"Institut f\u00fcr Biochemie, Fakult\u00e4t f\u00fcr Chemie und Pharmazie, 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Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alena","family":"Kussler","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0245cg223","id-type":"ROR","asserted-by":"publisher"}],"name":"Institut f\u00fcr Pharmazeutische Wissenschaften, Fakult\u00e4t f\u00fcr Chemie und Pharmazie, Albert-Ludwigs-Universit\u00e4t Freiburg","place":["Freiburg, Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8722-2893","authenticated-orcid":false,"given":"Oliver","family":"Einsle","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0245cg223","id-type":"ROR","asserted-by":"publisher"}],"name":"Institut f\u00fcr Biochemie, Fakult\u00e4t f\u00fcr Chemie und Pharmazie, Albert-Ludwigs-Universit\u00e4t Freiburg","place":["Freiburg, Germany"]},{"id":[{"id":"https:\/\/ror.org\/0245cg223","id-type":"ROR","asserted-by":"publisher"}],"name":"Centre for Integrative Biological Signalling 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Passaro Boltz-2: Towards accurate and efficient binding affinity prediction. bioRxiv [Preprint] (2025). https:\/\/doi.org\/10.1101\/2025.06.14.659707 (Accessed 26 January 2026).","DOI":"10.1101\/2025.06.14.659707"},{"key":"e_1_3_4_39_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41929-025-01425-3"},{"key":"e_1_3_4_40_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1529353"},{"key":"e_1_3_4_41_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi9603985"},{"key":"e_1_3_4_42_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi960026w"},{"key":"e_1_3_4_43_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi001645e"},{"key":"e_1_3_4_44_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi201003a"},{"key":"e_1_3_4_45_2","first-page":"125","article-title":"Biochemistry of methyl-coenzyme M reductase: The nickel metalloenzyme that catalyzes the final step in synthesis and the first step in anaerobic oxidation of the greenhouse gas methane","volume":"14","author":"Ragsdale S. 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Zhang F. Schuhmacher A. Kussler G. Layer O. Einsle Nitrogenase-like reductase CfbC\/D. Protein Data Bank. https:\/\/www.rcsb.org\/structure\/25AZ. Deposited 27 March 2026.","DOI":"10.2210\/pdb25az\/pdb"},{"key":"e_1_3_4_60_2","doi-asserted-by":"crossref","unstructured":"L. Zhang F. Schuhmacher A. Kussler G. Layer O. Einsle Nitrogenase-like reductase CfbC\/D. Electron Microscopy Data Bank. https:\/\/www.ebi.ac.uk\/emdb\/EMD-69985. 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