Open conformation of a flavocytochrome c3 fumarate reductase

Vicki Bamford, Paul S. Dobbin, David J. Richardson, Andrew M. Hemmings

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80 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1104-1107
Number of pages4
JournalNature Structural Biology
Issue number12
Publication statusPublished - 1999

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