The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile

Julius K. Demmer, Nilanjan Pal Chowdhury, Thorsten Selmer, Ulrich Ermler () and Wolfgang Buckel ()
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Julius K. Demmer: Max-Planck-Institut für Biophysik
Nilanjan Pal Chowdhury: Laboratorium für Mikrobiologie, Fachbereich Biologie and SYNMIKRO, Philipps-Universität
Thorsten Selmer: Fachbereich Chemie und Biotechnologie, FH Aachen
Ulrich Ermler: Max-Planck-Institut für Biophysik
Wolfgang Buckel: Laboratorium für Mikrobiologie, Fachbereich Biologie and SYNMIKRO, Philipps-Universität

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract The electron transferring flavoprotein/butyryl-CoA dehydrogenase (EtfAB/Bcd) catalyzes the reduction of one crotonyl-CoA and two ferredoxins by two NADH within a flavin-based electron-bifurcating process. Here we report on the X-ray structure of the Clostridium difficile (EtfAB/Bcd)4 complex in the dehydrogenase-conducting D-state, α-FAD (bound to domain II of EtfA) and δ-FAD (bound to Bcd) being 8 Å apart. Superimposing Acidaminococcus fermentans EtfAB onto C. difficile EtfAB/Bcd reveals a rotation of domain II of nearly 80°. Further rotation by 10° brings EtfAB into the bifurcating B-state, α-FAD and β-FAD (bound to EtfB) being 14 Å apart. This dual binding mode of domain II, substantiated by mutational studies, resembles findings in non-bifurcating EtfAB/acyl-CoA dehydrogenase complexes. In our proposed mechanism, NADH reduces β-FAD, which bifurcates. One electron goes to ferredoxin and one to α-FAD, which swings over to reduce δ-FAD to the semiquinone. Repetition affords a second reduced ferredoxin and δ-FADH−, which reduces crotonyl-CoA.

Date: 2017
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DOI: 10.1038/s41467-017-01746-3

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