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Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1

Nature Structural Biology volume 6, pages 1113–1117 (1999)Cite this article

Abstract

Fumarate respiration is one of the most widespread types of anaerobic respiration. The soluble fumarate reductase of Shewanella putrefaciens MR-1 is a periplasmic tetraheme flavocytochrome c. The crystal structures of the enzyme were solved to 2.9 Å for the uncomplexed form and to 2.8 Å and 2.5 Å for the fumarate and the succinate-bound protein, respectively. The structures reveal a flexible capping domain linked to the FAD-binding domain. A catalytic mechanism for fumarate reduction based on the structure of the complexed protein is proposed. The mechanism for the reverse reaction is a model for the homologous succinate dehydrogenase (complex II) of the respiratory chain. In flavocytochrome c fumarate reductase, all redox centers are in van der Waals contact with one another, thus providing an efficient conduit of electrons from the hemes via the FAD to fumarate.

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Figure 1: Protein fold of the soluble fumarate reductase.
Figure 2: Active site region.
Figure 3: Stereo representation of the redox centers in fumarate reductase.
Figure 4: Comparison of Shewanella soluble fumarate reductase with E.coli membrane-bound fumarate reductase and E. coli apo-LASPO.

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Acknowledgements

D.L. is a research assistant at the Fund for Scientific Research-Flanders. J.J.V.B. is indebted to the same institution for a research project and to the Bijzonder Onderzoeksfonds of the University of Ghent for a Concerted Research Action. Part of this work was supported by a grant from NIH. We thank S. Chapman and G. Reid for helpful discussions.

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Authors and Affiliations

  1. Department of Biochemistry, Laboratory of Protein Biochemistry and Protein Engineering, Physiology and Microbiology, K.L. Ledeganckstraat 35, Gent, 9000, Belgium

    David Leys & Jozef J. Van Beeumen

  2. Jet Propulsion Laboratory, California Institute of Technology, Pasadena, USA, California

    Alexandre S. Tsapin & Kenneth H. Nealson

  3. Department of Biochemistry, University of Arizona, Tucson, 85721, Arizona, USA

    Terrance E. Meyer & Michael A. Cusanovich

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  1. David Leys
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Correspondence to Jozef J. Van Beeumen.

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Leys, D., Tsapin, A., Nealson, K. et al. Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1. Nat Struct Mol Biol 6, 1113–1117 (1999). https://doi.org/10.1038/70051

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