Copper, zinc superoxide dismutase (Cu,Zn SOD (also commonly SOD1 for the cytosolic form))

Copper, zinc superoxide dismutase is a highly conserved, cytosolic, and sometimes extracellular enzyme that catalyzes the dismutation (disproportionation) of superoxide radicals (O₂⁻) into molecular oxygen and hydrogen peroxide, thus protecting cells from oxidative stress and associated molecular damage. The enzyme is a homodimer, with each ~16 kDa subunit containing a copper ion (for redox catalysis) and a zinc ion (for structural stability). It is essential for detoxifying superoxide generated by normal respiration and immune processes, and also has emerging roles in intracellular signaling, including transcriptional regulation in response to oxidative stress. Mutations in SOD1, especially those that confer toxic gain-of-function, are strongly implicated in the pathogenesis of familial ALS, and altered activity is linked to numerous disorders driven by oxidative damage, including cancer, diabetes, cardiovascular disease, and aging.

Other names

Superoxide dismutase 1SOD1Cu/Zn SODCopper-zinc superoxide dismutaseSuperoxide dismutase [Cu-Zn]SOD

Enzyme mimetics scavenge superoxide anions Stabilizers attempt to enhance SOD1’s natural activity Inhibitors may block electron transfer or metal binding, increasing superoxide toxicity Chelators may remove copper/zinc to inhibit or modulate its function Drugs may indirectly affect SOD1 function by modulating oxidative stress pathways