S95C substitution in CuZn-SOD of Ipomoea carnea: impact on the structure, function and stability
作者： Panchanand Mishra , Suresh Satpati , Sudhira Kumar Baral , Anshuman Dixit , Surendra Chandra Sabat
DOI: 10.1039/C6MB00458J
关键词: Stereochemistry 、 Circular dichroism 、 Chemistry 、 Cysteine 、 Protein subunit 、 Ipomoea carnea 、 Dismutase 、 Peroxidase 、 Serine 、 Superoxide dismutase
摘要: Superoxide dismutase (SOD) in general is a unique homo-dimeric enzyme that can scavenge toxic superoxide radicals by dismutation reaction. In IcSOD (Ipomoea carnea SOD), the presence of cysteine (Cys) plays an essential role protein behaviour. This study analysed Cys modulating stability and kinetic properties IcSOD. To investigate significance dimeric structure structure/function relationship CuZn-SODs, we have substituted conserved serine (Ser95Cys) Ipomoea CuZn-SOD. The results demonstrate this mutation leads to increase strength, as reflected size exclusion chromatography, differential scanning calorimetry, high-temperature circular dichroism spectroscopy measurements. mutant form, compared native enzyme, shows relatively low tendency form aggregates but encountered reduction both peroxidase activities. provides new mechanistic insight into free CuZn-SODs such may be used strength. Protein docking molecular dynamics simulations further Ser95Cys substitution CuZn-SOD creation subunit interface resulting increased strength protein.
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