Molecular Playground/ Copper-Zinc Superoxide Dismutase

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Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)

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, leading to a destabilized protein structure ^[2]. 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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Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains one atom of Copper (Cu), and one atom of Zinc (Zn) (highlight Cu and Zn). Each Cu is bound to four nitrogen atoms (show his His 46, 48, 63, 120) and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight hydrophobic interface between the monomers (highlight hydrophobic interface of the dimer) and “the two halves of the βeta (β)- barrel core” ( insert reference).

References

1. ↑ Superoxide dismutase in Wikipedia
2. ↑ ^{2.0 2.1} 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