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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) radical into ordinary 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. 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 a different mechanism to prevent damage from reactive O−
2.
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Superoxide dismutase [Cu-Zn] also known as superoxide dismutase 1 or hSod1 is an enzyme that in humans is encoded by the SOD1 gene, located on chromosome 21. SOD1 is one of three human superoxide dismutases. It is implicated in apoptosis, familial amyotrophic lateral sclerosis and Parkinson's disease.
Superoxide dismutase 2, mitochondrial (SOD2), also known as manganese-dependent superoxide dismutase (MnSOD), is an enzyme which in humans is encoded by the SOD2 gene on chromosome 6. A related pseudogene has been identified on chromosome 1. Alternative splicing of this gene results in multiple transcript variants. This gene is a member of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. This protein binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in this gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer.
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Nickel superoxide dismutase (Ni-SOD) is a metalloenzyme that, like the other superoxide dismutases, protects cells from oxidative damage by catalyzing the disproportionation of the cytotoxic superoxide radical to hydrogen peroxide and molecular oxygen. Superoxide is a reactive oxygen species that is produced in large amounts during photosynthesis and aerobic cellular respiration. The equation for the disproportionation of superoxide is shown below:
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Türkan Haliloğlu is a Turkish biochemist researching biopolymers, computational structural biology, protein dynamics, binding and folding of proteins, and protein interactions. She is a professor in the department of chemical engineering and director of the polymer research center at the Boğaziçi University.
Katrina T. Forest is an American biologist who is the EB Fred Professor of Bacteriology and Chair in the Department of Bacteriology at the University of Wisconsin–Madison. Her research considers the use of structural biology to better understand pathogenesis. Forest is a Fellow of the American Society for Microbiology.
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References
- ↑ "Getzoff, Elizabeth". vivo.scripps.edu. Retrieved 2020-03-07.
- ↑ "Skaggs Institute for Chemical Biology | Scripps Research". www.scripps.edu. Retrieved 2020-03-07.
- ↑ "ELIZABETH D. GETZOFF LABORATORY". www.scripps.edu. Retrieved 2020-03-07.
- ↑ pubmeddev. "Elizabeth D. Getzoff - PubMed - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2020-03-07.
- 1 2 3 4 Google Scholar Author page, Accessed August 17, 2020
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