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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Open conformation of a flavocytochrome c3 fumarate reductase.

Fumarate reductases and succinate dehydrogenases play central roles in the metabolism of eukaryotic and prokaryotic cells. A recent medium resolution structure of the Escherichia coli fumarate reductase ( Frd) has revealed the overall organization of the membrane-bound complex. Here we present the first high resolution X-ray crystal structure of a water-soluble bacterial fumarate reductase in an open conformation. This structure reveals a mobile domain that modulates substrate access to the active site and provides new insights into the mechanism of this widespread and important family of FAD-containing respiratory proteins.[1]


  1. Open conformation of a flavocytochrome c3 fumarate reductase. Bamford, V., Dobbin, P.S., Richardson, D.J., Hemmings, A.M. Nat. Struct. Biol. (1999) [Pubmed]
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