Metal-dependent oxidoreductase

Metal-dependent oxidoreductases represent a broad and essential class of enzymes that utilize metal ions—such as iron, zinc, copper, manganese, or molybdenum—as cofactors to facilitate oxidation-reduction reactions (PubMed: 10736164). These enzymes are integral to a wide array of biological processes, including cellular respiration, the neutralization of reactive oxygen species, and the biosynthesis of DNA precursors (UniProt: P00325). For instance, xanthine oxidase requires molybdenum to catalyze the oxidation of hypoxanthine to uric acid, while superoxide dismutases rely on metals like copper and zinc to protect cells from oxidative damage (PubMed: 11340053). In a clinical context, these enzymes are significant therapeutic targets; drugs like allopurinol and hydroxyurea exert their effects by inhibiting specific metal-dependent oxidoreductases to treat conditions such as gout and certain cancers, respectively (StatPearls: NBK499945). However, because many of these enzymes share similar metal-binding motifs, developing highly selective inhibitors remains a challenge, often leading to potential safety concerns regarding off-target metal chelation or the disruption of essential metabolic pathways (PubMed: 10665501).

Other names

Metallo-oxidoreductaseMetal-containing oxidoreductaseMetalloenzyme oxidoreductase

Inhibition of enzymatic activity through competitive binding at the active site or interference with metal cofactor coordination.