Superoxide dismutase (SOD) is an enzyme that catalyzes the disproportionation of superoxide radicals into oxygen and hydrogen peroxide. It is widely found in animals, plants, and microorganisms, and plays a crucial role as an antioxidant by protecting cells from oxidative damage caused by reactive oxygen species.
First discovered by Irving Fridovich and Joe McCord, SOD was initially considered to be a group of metal-containing proteins with unknown functions. Today, we know that SOD exists in several forms, depending on the cofactors it uses—such as manganese, iron, copper, and zinc. These enzymes are essential for maintaining cellular redox balance and preventing oxidative stress.
In humans, there are three main types of SOD: SOD1, located in the cytoplasm; SOD2, found in the mitochondria; and SOD3, which is extracellular. SOD1 and SOD3 contain copper and zinc at their active sites, while SOD2 relies on manganese. These genes are mapped to chromosome 21, highlighting their importance in human biology.
As one of the primary reactive oxygen species, superoxide radicals can cause significant damage if left unchecked. SOD plays a key role in neutralizing these radicals, making it vital for cellular health. Studies on genetically modified mice have shown the critical role of SOD in development and disease resistance.
For example, SOD2-deficient mice die within days due to severe oxidative stress, while SOD1-deficient mice develop various pathologies, including liver cancer, early cataracts, and reduced lifespan. In contrast, SOD3-deficient mice appear normal but are more susceptible to high-oxygen environments. Mice lacking SOD are highly vulnerable to toxins like paraquat and diquat, which increase superoxide production and lead to rapid death.
Similar findings have been observed in other organisms, such as fruit flies and nematodes, where SOD deficiencies result in shortened lifespans or developmental issues. In yeast, SOD1 and SOD2 mutations lead to poor growth under anaerobic conditions and reduced viability.
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