Molecular Playground/ Copper-Zinc Superoxide Dismutase

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The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O<sub>2</sub><sup>-</sup>) anion into molecular oxygen (O<sub>2</sub>) and hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref>PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure (reference). This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.
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The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O<sub>2</sub><sup>-</sup>) anion into molecular oxygen (O<sub>2</sub>) and hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref>PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure <ref>PMID: 16828895</ref>. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.
'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''

Revision as of 20:02, 20 January 2011

The important function of Cu/ Zn superoxide dismutase (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)[1]. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis (ALS) and diabetes[2]. One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure [3]. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)

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References

  1. ↑ Superoxide dismutase in Wikipedia
  2. ↑ Culotta VC, Yang M, O'Halloran TV. Activation of superoxide dismutases: putting the metal to the pedal. Biochim Biophys Acta. 2006 Jul;1763(7):747-58. Epub 2006 May 17. PMID:16828895 doi:10.1016/j.bbamcr.2006.05.003
  3. ↑ Culotta VC, Yang M, O'Halloran TV. Activation of superoxide dismutases: putting the metal to the pedal. Biochim Biophys Acta. 2006 Jul;1763(7):747-58. Epub 2006 May 17. PMID:16828895 doi:10.1016/j.bbamcr.2006.05.003

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Shaynah Browne, Michal Harel

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