Open conformation of a flavocytochrome c3 fumarate reductase.
作者： Andrew M. Hemmings , Vicki Bamford , Paul S. Dobbin , David J. Richardson
DOI: 10.1038/70039
关键词: Biochemistry 、 Oxidoreductase 、 Metabolism 、 Peptide sequence 、 Protein structure 、 Structure–activity relationship 、 Biology 、 Stereochemistry 、 Escherichia coli 、 Active site 、 Fumarate reductase
摘要: Fumarate reductases and succinate dehydrogenases play central roles in the metabolism of eukaryotic prokaryotic cells. A recent medium resolution structure Escherichia coli fumarate reductase (Frd) has revealed overall organization membrane-bound complex. Here we present first high X-ray crystal a water-soluble bacterial an open conformation. This reveals mobile domain that modulates substrate access to active site provides new insights into mechanism this widespread important family FAD-containing respiratory proteins.
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