Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution

C. Roy D. Lancaster (), Achim Kröger, Manfred Auer and Hartmut Michel ()
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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
Hartmut Michel: Max-Planck-Institut für Biophysik

Nature, 1999, vol. 402, issue 6760, 377-385

Abstract: 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.

Date: 1999
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DOI: 10.1038/46483

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