Biochemistry · Enzyme
Superoxide dismutase (SOD) !
Superoxide dismutase turns the superoxide radical into hydrogen peroxide and oxygen; it is the first antioxidant line.
Updated 2026-11-01
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Key facts
- 2 O₂•⁻ + 2 H⁺ → H₂O₂ + O₂; catalase or glutathione peroxidase then remove the H₂O₂.
- Three forms: SOD1 with copper and zinc (cytosol), SOD2 with manganese (mitochondrial matrix, next to the chain) and SOD3 (extracellular).
- It is one of the fastest enzymes known: it works almost at the rate of diffusion.
- Copper changes valence in the reaction; zinc stabilises the structure.
Regulation
- SOD2 is induced by inflammatory cytokines and oxidative stress.
- It needs copper, zinc or manganese depending on the form: deficiency lowers activity.
Inhibitors and toxins
- Diethyldithiocarbamate (copper chelator, experimental use)
Clinical notes
- SOD1 variants cause part of familial amyotrophic lateral sclerosis; the damage comes from the misfolded protein, not only from lost activity.
- Neutrophils use superoxide to kill microbes: SOD turns it into H₂O₂, which myeloperoxidase converts to hypochlorite.
Related
- Catalase
- Glutathione peroxidase (GPX)
- Reactive oxygen species and antioxidants
- Complex I (NADH dehydrogenase)
- Complex III (cytochrome bc₁)
Test yourself
Think of the answer, then tap the question to see it.
What reaction does superoxide dismutase catalyse?
It turns two superoxides into H₂O₂ and O₂; catalase and glutathione peroxidase then remove the H₂O₂.
Which metal does mitochondrial SOD contain?
Manganese (SOD2); the cytosolic form (SOD1) has copper and zinc.
Which neurological disease is linked to SOD1 variants?
Familial amyotrophic lateral sclerosis.
Educational information, not medical advice. For any symptom, see a health professional.
Sources: SOD1: Superoxide dismutase [Cu-Zn] (human) (UniProt, 2026); SOD2: Superoxide dismutase [Mn], mitochondrial (human) (UniProt, 2026); SOD1 gene: MedlinePlus Genetics (MedlinePlus, US National Library of Medicine, 2026); Amyotrophic lateral sclerosis: MedlinePlus Genetics (MedlinePlus, US National Library of Medicine, 2026); 2C9V: Atomic resolution structure of Cu-Zn Human Superoxide dismutase (RCSB Protein Data Bank, 2026).
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