Molecular Playground/ Copper-Zinc Superoxide Dismutase
From Proteopedia
| Line 5: | Line 5: | ||
{{Clear}} | {{Clear}} | ||
--> | --> | ||
| - | The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD)is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide ( | + | 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 (O2) and hydrogen peroxide (H2O2)<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 (ALS) (Wikipedia add reference) and diabetes. (reference). 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. |
'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)''' | '''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)''' | ||
Revision as of 19:44, 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) (Wikipedia add reference) and diabetes. (reference). 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.
Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)
|
