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

Demmer, Julius K., Bertsch, Johannes, Öppinger, Christian, Wohlers, Hannah, Kayastha, Kanwal, Demmer, Ulrike, Ermler, Ulrich, Müller, Volker·2018·FEBS Letters
DOI 10.1002/1873-3468.12971
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Abstract

Flavin‐based electron bifurcation (FBEB) is a recently discovered mode of energy coupling in anaerobic microorganisms. The electron‐bifurcating caffeyl‐CoA reductase (Car CDE) 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 Car CDE(∆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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Metadata

Authors
Demmer, J. K., Bertsch, J., Öppinger, C., Wohlers, H., Kayastha, K., Demmer, U., Ermler, U., & Müller, V.
Affiliations
  • Max‐Planck‐Institut für Biophysik Frankfurt am Main Germany
  • Department of Molecular Microbiology and Bioenergetics Institute of Molecular Biosciences Johann Wolfgang Goethe‐Universität Frankfurt am Main Germany
Venue
FEBS Letters
Publisher
Wiley
Published
2018-02
Volume
592
Issue
3
Pages
332-342
ISSN
  • 0014-5793
  • 1873-3468
DOI
10.1002/1873-3468.12971
Cited by
41
References
3
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Funders
Deutsche Forschungsgemeinschaft

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