| Description | In bacteria two distinct, membrane-bound, enzyme complexes are responsible for the interconversion of fumarate and succinate ( ): fumaratereductase (Frd) is used in anaerobic growth, and succinate dehydrogenase (Sdh) is used in aerobic growth. Both complexes consist of two main components: a membrane-extrinsic component composed of a FAD-binding flavoprotein and an iron-sulphur protein; and an hydrophobic component composed of a membrane anchor protein and/or a cytochrome B. In eukaryotes mitochondrial succinate dehydrogenase (ubiquinone) ( ) is an enzyme composed of two subunits: a FAD flavoprotein and and iron-sulphur protein. The flavoprotein subunit is a protein of about 60 to 70 Kd to which FAD is covalently bound to a histidine residue which is located in the N-terminal section of the protein [ ]. The sequence around that histidine is well conserved in Frd and Sdh from various bacterial and eukaryotic species [].The terms succinate dehydrogenase and fumarate reductase may be used interchangeably in certain systems. However, a number of species have distinct complexes, with the fumarate reductase active under anaerobic conditions. This model represents the fumarate reductase flavoprotein subunit from several such species in which a distinct succinate dehydrogenase is also found. | Name | Fumarate reductase, flavoprotein subunit |
| Short Name | Fum_red_fp | Type | Family |
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