Superoxide dismutase and related antioxidant enzymes (SOD)

Superoxide dismutase (SOD) and related antioxidant enzymes, including catalase and glutathione peroxidase, represent the primary enzymatic defense against oxidative damage in biological systems (McCord & Fridovich, 1969). These enzymes function by scavenging reactive oxygen species (ROS) like superoxide radicals and hydrogen peroxide, which otherwise cause lipid peroxidation, protein denaturation, and DNA damage (UniProt). SOD specifically converts superoxide into hydrogen peroxide, which is then further detoxified by catalase or glutathione peroxidase into water and oxygen (PubMed). Clinical interest in these targets is high due to their role in neurodegenerative conditions like Amyotrophic Lateral Sclerosis (ALS), where SOD1 mutations are a known cause, as well as in inflammatory and cardiovascular diseases (Rosen et al., 1993). Pharmacological interventions include enzyme replacement therapies, small-molecule SOD mimics, and antisense oligonucleotides like tofersen designed to modulate enzyme levels (FDA; ClinicalTrials.gov). However, therapeutic application is often limited by the short half-life of protein-based drugs and the risk of disrupting delicate redox signaling (StatPearls).

Other names

SODAntioxidant enzymesReactive oxygen species scavengersSuperoxide:superoxide oxidoreductase

Catalytic dismutation of superoxide radicals into oxygen and hydrogen peroxide, followed by the reduction of hydrogen peroxide to water by associated antioxidant enzymes.