Fe Superoxide Dismutase (Fe SOD) is an enzyme that serves as a crucial antioxidant defense mechanism in many living organisms. It belongs to the superoxide dismutase family of enzymes and is characterized by its dependency on iron (Fe) as a cofactor. Fe SOD primarily functions to catalyze the conversion of superoxide radicals (O2·-) into molecular oxygen (O2) and hydrogen peroxide (H2O2).
The enzyme is composed of a homodimer structure, where each subunit consists of a barrel-shaped core composed of eight anti-parallel β-strands surrounded by eight α-helices. These β-strands are responsible for binding iron cofactors within each subunit, which are essential for the enzyme's functionality.
Fe SOD plays a pivotal role in protecting cells against oxidative stress caused by the accumulation of harmful superoxide radicals, which can lead to oxidative damage and contribute to various diseases and aging processes. By efficiently dismutating superoxide radicals into less reactive molecules, Fe SOD helps maintain the balance of reactive oxygen species (ROS) in cells, preventing potential oxidative damage to cellular components such as proteins, lipids, and DNA.
This enzyme is found in various organisms, including bacteria, fungi, plants, and animals, highlighting its evolutionary importance. Fe SOD also demonstrates its significance in the metabolic processes of nitrogen fixation and symbiotic nitrogen fixation in certain bacteria and plants, respectively.
Overall, Fe Superoxide Dismutase constitutes a fundamental element of the cellular antioxidant defense system, acting as a critical enzyme in maintaining redox homeostasis and protecting organisms against oxidative stress-induced damage.
