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Citation: Li Wen-Zhong, Miao Fang-Ming. Solvation Interaction and Stability of Modified Superoxide Dismutase[J]. Acta Physico-Chimica Sinica, ;1998, 14(04): 289-292. doi: 10.3866/PKU.WHXB19980401 shu

Solvation Interaction and Stability of Modified Superoxide Dismutase

1.
Institute of Chemical Crystallography,Tianjin Normal University,Tianjin 300074 P.R.China

Received Date: 15 December 1997
Available Online: 15 April 1998

The stability of Copper, Zinc superoxide dismutase increases remarkably when the lysines on the surface of the enzyme are modified. The fmite difference solution to the Poisson-Boltzman equation (FDPB) method is used to calculate the electrostatic interaction between solution and enzyme. The results show that the reaction field energy of SOD is reduced by about,1270kJ•mol-1 after modification.
- Enzyme stability,
- Finite difference,
- Superoxide desmutase,
- Chemical modification,
- Reaction field energy
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