The pos$ile structxai basis of the specific i&Story action of cuprein on the autoxidation of catfqchola+ne wasexamined. The chjro&al properties -\_ of the native enzyme were compared with both tlk denatukd tid the apo-' protein and-i& stiperoxide-disnutasease-active Cu(T$r)p. A&rt froth the reduc-'
Chemical aspects of structure, function and evolution of superoxide dismutases
β Scribed by J.V Bannister
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 247 KB
- Volume
- 79
- Category
- Article
- ISSN
- 0020-1693
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## Abstract Superoxide dismutases are essential enzymes involved in detoxification of reactive oxygen by dismutation of the superoxide radical anion. A class of nickel containing superoxide dismutases has been described for streptomycetes and cyanobacteria. __In silico__ analysis was used to study
Mutation of arginine (Arg) 143 with Ile in the monomeric mutant (Phe50Glu, Gly51Glu, Val148Lys, Ile151Lys) of copper-zinc superoxide dismutase (R143I M4SOD, where M4SOD is the above mutant) leads to a protein with low copper content. Cobalt(II) binds the demetalized protein with a low and comparable