{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sucharitakul J"],"funding":["Faculty of Dentistry, Chulalongkorn University","Chulalongkorn University","National Research Council of Thailand","Vidyasirimedhi Institute of Science and Technology"],"pagination":["110727"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12552937"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["301(10)"],"pubmed_abstract":["Electron transfer flavoprotein (EtfAB, with α-FAD and β-FAD) and tetrameric butyryl-CoA dehydrogenase (Bcd, with δ-FAD in each subunit) from Acidaminococcus fermentans catalyze electron bifurcation which reduces low potential ferredoxin (Fd) and high potential crotonyl-CoA using NADH as an electron donor. Our previous rapid kinetic studies have demonstrated \"pseudo-electron bifurcation\" where NADH and two EtfAB molecules generate EtfA<sub>SQ</sub>B (A<sub>SQ</sub> contains α-FAD<sup>•-</sup>) and the charge-transfer complex of EtfA<sub>SQ</sub>B<sub>HQ</sub>:NAD<sup>+</sup> (B<sub>HQ</sub> contains β-FADH<sup>-</sup>). Since the radical in EtfA<sub>SQ</sub>B inhibits the further reduction of β-FAD with NADH, the question arises as to how the five components of the complete system interact "],"journal":["The Journal of biological chemistry"],"pubmed_title":["Kinetic mechanisms of electron bifurcation with electron transfer flavoprotein, NADH, butyryl-CoA dehydrogenase, and ferredoxin reveal a semiquinone cycle."],"pmcid":["PMC12552937"],"funding_grant_id":["196844","B05F640089","N42A680106","PHD/0015/2561"],"pubmed_authors":["Buckel W","Chaiyen P","Pornsuwan S","Intasian P","Mangkalee M","Ermler U","Sucharitakul J"],"additional_accession":[]},"is_claimable":false,"name":"Kinetic mechanisms of electron bifurcation with electron transfer flavoprotein, NADH, butyryl-CoA dehydrogenase, and ferredoxin reveal a semiquinone cycle.","description":"Electron transfer flavoprotein (EtfAB, with α-FAD and β-FAD) and tetrameric butyryl-CoA dehydrogenase (Bcd, with δ-FAD in each subunit) from Acidaminococcus fermentans catalyze electron bifurcation which reduces low potential ferredoxin (Fd) and high potential crotonyl-CoA using NADH as an electron donor. Our previous rapid kinetic studies have demonstrated \"pseudo-electron bifurcation\" where NADH and two EtfAB molecules generate EtfA<sub>SQ</sub>B (A<sub>SQ</sub> contains α-FAD<sup>•-</sup>) and the charge-transfer complex of EtfA<sub>SQ</sub>B<sub>HQ</sub>:NAD<sup>+</sup> (B<sub>HQ</sub> contains β-FADH<sup>-</sup>). Since the radical in EtfA<sub>SQ</sub>B inhibits the further reduction of β-FAD with NADH, the question arises as to how the five components of the complete system interact ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-10T05:20:05.009Z","creation":"2026-06-10T03:07:14.39Z"},"accession":"S-EPMC12552937","cross_references":{"pubmed":["40967436"],"doi":["10.1016/j.jbc.2025.110727"]}}