SOD1 (147-153) human – Other Categories

The SOD1 homodimer forms a β-barrel and contains an intramolecular disulphide bond and a binuclear Cu/Zn site in each subunit. This Cu/Zn site holds a copper and zinc ion and is responsible for catalysing the disproportionation of ROS, namely superoxide to hydrogen peroxide and dioxygen. In binding to copper and zinc ions, SOD1 is one of three superoxide dismutases responsible for destroying free superoxide radicals. The clinical relevance of SOD1 is related to its function in regulating ROS in the mitochondria of cells. Most notably, SOD1 is a crucial enzyme involved in ROS release during oxidative stress by ischemia-reperfusion injury, specifically in the myocardium as part of ischemic heart disease. During ischemia reperfusion, ROS release substantially contribute to the cell damage and death via a direct effect on the cell as well as via apoptotic signals. SOD1 is known to have a capacity to limit the detrimental effects of ROS. As such, SOD1 is important for its cardioprotective effects.