Structure of a human Mn superoxide dismutase 2 tetramer[1]
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1.15.1.1
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9054-89-1
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Superoxide dismutase (SOD, EC 1.15.1.1) is an enzyme that alternately catalyzes the dismutation (or partitioning) of the superoxide (O− 2) anion radical into normal molecular oxygen (O2) and hydrogen peroxide (H 2O 2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage.[2] Hydrogen peroxide is also damaging and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use intracellular manganese to prevent damage from reactive O− 2.[3][4]
^Cite error: The named reference pmid8605177 was invoked but never defined (see the help page).
^Hayyan M, Hashim MA, AlNashef IM (March 2016). "Superoxide Ion: Generation and Chemical Implications". Chemical Reviews. 116 (5): 3029–3085. doi:10.1021/acs.chemrev.5b00407. PMID 26875845.
^Archibald FS, Fridovich I (1981). "Manganese and Defenses against Oxygen Toxicity in Lactobacillus plantarum". Journal of Bacteriology. 145 (1): 442–451. doi:10.1128/jb.145.1.442-451.1981. PMC 217292. PMID 6257639.
^Peacock T, Hassan HM (2021). "Role of the Mn-Catalase in Aerobic Growth of Lactobacillus plantarum ATCC 14431". Applied Microbiology. 1 (3): 615–625. doi:10.3390/applmicrobiol1030040. S2CID 245379268.
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