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Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution

Author

Listed:
  • C. Roy D. Lancaster

    (Max-Planck-Institut für Biophysik)

  • Achim Kröger

    (Johann Wolfgang Goethe-Universität, Institut für Mikrobiologie)

  • Manfred Auer

    (Max-Planck-Institut für Biophysik
    NYU Medical Center)

  • Hartmut Michel

    (Max-Planck-Institut für Biophysik)

Abstract

Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalysed by the related complex II of the respiratory chain (succinate dehydrogenase). Here we describe the crystal structure at 2.2 Å resolution of the three protein subunits containing fumarate reductase from the anaerobic bacterium Wolinella succinogenes. Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide prosthetic group. Subunit B contains three iron–sulphur centres. The menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules. On the basis of the structure, we propose a pathway of electron transfer from the dihaem cytochrome b to the site of fumarate reduction and a mechanism of fumarate reduction. The relative orientations of the soluble and membrane-embedded subunits of succinate:quinone oxidoreductases appear to be unique.

Suggested Citation

  • C. Roy D. Lancaster & Achim Kröger & Manfred Auer & Hartmut Michel, 1999. "Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution," Nature, Nature, vol. 402(6760), pages 377-385, November.
    • Handle: RePEc:nat:nature:v:402:y:1999:i:6760:d:10.1038_46483
    DOI: 10.1038/46483
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