| Type: | Binding_site | Name: | Fumarate reductase/succinate dehydrogenase, FAD-binding site |
| Description: | In bacteria two distinct, membrane-bound, enzyme complexes are responsible for the interconversion of fumarate and succinate (): fumarate reductase (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 aniron-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-sulphurprotein.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-terminalsection of the protein []. The sequence around that histidine is wellconserved in Frd and Sdh from various bacterial and eukaryotic species []. | Short Name: | FRD_SDH_FAD_BS |
