<p> Glutathione reductase is an enzyme that catalyzes the two electron reduction of oxidized glutathione. It belongs to the FAD flavoprotein family of pyridine nucleotide-disulphide oxidoreductases. Other family members include mercuric ion reductase, trypanothione reductase, lipoamide dehydrogenase, thioredoxin reductase, alkyl hydroperoxide reductase). FAD is used to shuttle electrons from NADPH to substrate. In general the family members undergo dithiol/disulphide interchange between the enzyme and substrate. To date, 3D structures of glutathione reductase [<cite idref="PUB00003219"/>], thioredoxin reductase [<cite idref="PUB00004100"/>], mercuric reductase [<cite idref="PUB00004099"/>], lipoamide dehydrogenase [<cite idref="PUB00003272"/>], and trypanothione reductase [<cite idref="PUB00004756"/>] have been solved. The enzymes share similar tertiary structures based on a doubly-wound alpha/beta fold, but the relative orientations of their FAD- and NAD(P)H-binding domains may vary significantly.</p> Glutathione-disulphide reductase-related