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, playing 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 thought to be a group of metal-containing proteins with unknown functions. Over time, it became clear that different forms of SOD exist, depending on the metal cofactors they require. For example, some types use manganese or iron, while others rely on copper and zinc.
In humans, there are three main forms of SOD: SOD1, located in the cytoplasm; SOD2, found in the mitochondria; and SOD3, which resides outside the cell. SOD1 and SOD3 contain copper and zinc at their active sites, whereas SOD2 contains manganese. These genes are all located on chromosome 21.
As one of the primary reactive oxygen species, superoxide radicals can cause significant cellular damage if left unchecked. Therefore, SOD plays a vital role in the body's defense against oxidative stress. Studies on genetically modified mice have shown the importance of SOD in maintaining health. For instance, SOD2-deficient mice die within days due to severe oxidative stress, while SOD1-deficient mice show various pathologies such as liver cancer, muscle loss, early cataracts, and reduced lifespan.
SOD3-deficient mice generally appear normal but are more vulnerable to high oxygen exposure. Mice lacking any form of SOD are more sensitive to toxins like paraquat and diquat, which increase superoxide production and lead to higher mortality rates. Similar results have been observed in fruit flies and nematodes, where SOD deficiencies lead to shortened lifespans or developmental issues.
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