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  Molecular basis of the flavin‐based electron‐bifurcating caffeyl‐CoA reductase reaction

Demmer, J. K., Bertsch, J., Öppinger, C., Wohlers, H., Kayastha, K., Demmer, U., et al. (2018). Molecular basis of the flavin‐based electron‐bifurcating caffeyl‐CoA reductase reaction. FEBS Letters, 592(3), 332-342. doi:10.1002/1873-3468.12971.

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 Creators:
Demmer, Julius K.1, Author              
Bertsch, Johannes2, Author
Öppinger, Christian2, Author
Wohlers, Hannah2, Author
Kayastha, Kanwal1, Author              
Demmer, Ulrike1, Author              
Ermler, Ulrich1, Author              
Müller, Volker2, Author
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe‐Universität Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: acetogenic bacteria; bioenergetics; crystal structure; electron-transferring flavoprotein/acyl-CoA dehydrogenase; ferredoxin; flavin-based electron bifurcation
 Abstract: Flavin‐based electron bifurcation (FBEB) is a recently discovered mode of energy coupling in anaerobic microorganisms. The electron‐bifurcating caffeyl‐CoA reductase (CarCDE) catalyzes the reduction of caffeyl‐CoA and ferredoxin by oxidizing NADH. The 3.5 Å structure of the heterododecameric Car(CDE)4 complex of Acetobacterium woodii, presented here, reveals compared to other electron‐transferring flavoprotein/acyl dehydrogenase family members an additional ferredoxin‐like domain with two [4Fe–4S] clusters N‐terminally fused to CarE. It might serve, in vivo, as specific adaptor for the physiological electron acceptor. Kinetic analysis of a CarCDE(∆Fd) complex indicates the bypassing of the ferredoxin‐like domain by artificial electron acceptors. Site‐directed mutagenesis studies substantiated the crucial role of the C‐terminal arm of CarD and of ArgE203, hydrogen‐bonded to the bifurcating FAD, for FBEB.

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Language(s): eng - English
 Dates: 2017-11-162018-01-042018-02-012018-02
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/1873-3468.12971
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 592 (3) Sequence Number: - Start / End Page: 332 - 342 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501