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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Thermal Dissociation and Conformational Lock of Superoxide Dismutase

  • Hong, J. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Moosavi-Movahedi, A.A. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Ghourchian, H. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Amani, M. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Amanlou, M. (Department of Medicinal Chemistry, Tehran University of Medical Sciences) ;
  • Chilaka, F.C. (Department of Biochemistry, University of Nigeria)
  • Published : 2005.09.30
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Abstract

The kinetics of thermal dissociation of superoxide dismutase (SOD) was studied in 0.05 M Tris-HCl buffer at pH 7.4 containing $10^{-4}\;M$ EDTA. The number of conformational locks and contact areas and amino acid residues of dimers of SOD were obtained by kinetic analysis and biochemical calculation. The cleavage bonds between dimers of SOD during thermal dissociation and type of interactions between specific amino acid residues were also simulated. Two identical contact areas between two subunits were identified. Cleavage of these contact areas resulted in dissociation of the subunits, with destruction of the active centers, and thus, lost of activity. It is suggested that the contact areas interact with active centers by conformational changes involving secondary structural elements.

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References

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