sod 2

Superoxide Dismutase (SOD2) belongs to the iron manganese superoxide dismutase family. SOD2 is a mitochondrial matrix protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 transforms toxic superoxide, a byproduct of the mitochondrial electron transport chain into hydrogen peroxide and diatomic oxygen. It is reported that oxidative stress plays an essential role in the development of breast cancer, while SOD2 is one of the primary enzymes that directly convert potential harmful oxidizing species to harmless metabolites.

Superoxide Dismutase (SOD2) is a number of the iron manganese superoxide dismutase family. SOD2 is a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. The SOD2 protein transforms toxic superoxide and a byproduct of the mitochondrial electron transport chain into hydrogen peroxide and diatomic oxygen. Genetic variation in SOD2 is associated with microvascular complications of diabetes type 6 (MVCD6), idiopathic cardiomyopathy (IDC), sporadic motor neuron disease, and cancer. SOD2 destroys superoxide anion radicals which are usually produced within the cells and which are toxic to biological systems.

Superoxide dismutases (SOD) are important anti-oxidant enzymes that guard against superoxide toxicity. In humans, as in all mammals and most chordates, three forms of superoxide dismutase (SOD) are present: SOD1 is located in the cytoplasm, SOD2 in the mitochondria, and SOD3 is extracellular. Mitochondrial superoxide dismutase [SOD; manganese SOD (MnSOD) or SOD2] neutralizes highly reactive superoxide radical (O•-2), the first member in the plethora of mitochondrial reactive oxygen species.