Back to Search
Start Over
Towards Al3+-Induced Manganese-Containing Superoxide Dismutase Inactivation and Conformational Changes: An Integrating Study with Docking Simulations
- Source :
- Enzyme Research, Vol 2011 (2011)
- Publication Year :
- 2011
- Publisher :
- Hindawi Limited, 2011.
-
Abstract
- Superoxide dismutase (SOD, EC 1.15.1.1) plays an important antioxidant defense role in skins exposed to oxygen. We studied the inhibitory effects of Al3+ on the activity and conformation of manganese-containing SOD (Mn-SOD). Mn-SOD was significantly inactivated by Al3+ in a dose-dependent manner. The kinetic studies showed that Al3+ inactivated Mn-SOD follows the first-order reaction. Al3+ increased the degree of secondary structure of Mn-SOD and also disrupted the tertiary structure of Mn-SOD, which directly resulted in enzyme inactivation. We further simulated the docking between Mn-SOD and Al3+ (binding energy for Dock 6.3: −14.07 kcal/mol) and suggested that ASP152 and GLU157 residues were predicted to interact with Al3+, which are not located in the Mn-contained active site. Our results provide insight into the inactivation of Mn-SOD during unfolding in the presence of Al3+ and allow us to describe a ligand binding via inhibition kinetics combined with the computational prediction.
Details
- Language :
- English
- ISSN :
- 20900414
- Volume :
- 2011
- Database :
- OpenAIRE
- Journal :
- Enzyme Research
- Accession number :
- edsair.dedup.wf.001..fc43d883eaa7ffe53f424489bd7b8e67