In bacteria two distinct, membrane-bound, enzyme complexes are responsible for
the interconversion of fumarate and succinate (EC 1.3.99.1): 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 an
iron-sulfur protein; and an hydrophobic component composed of a membrane
anchor protein and/or a cytochrome B.
In eukaryotes mitochondrial succinate dehydrogenase (ubiquinone) (EC 1.3.5.1)
is an enzyme composed of two subunits: a FAD flavoprotein and and iron-sulfur
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 [1]. The sequence around that histidine is well
conserved in Frd and Sdh from various bacterial and eukaryotic species [2] and
can be used as a signature pattern.
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