Role of the dimeric structure in Cu,Zn superoxide dismutase. pH-dependent, reversible denaturation of the monomeric enzyme from Escherichia coli.

@article{Battistoni1998RoleOT,
  title={Role of the dimeric structure in Cu,Zn superoxide dismutase. pH-dependent, reversible denaturation of the monomeric enzyme from Escherichia coli.},
  author={Andrea Battistoni and S Folcarelli and Laura Cervoni and Francesca Polizio and Alessandro Desideri and Anna Giartosio and Giuseppe Rotilio},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 10},
  pages={5655-61}
}
To investigate the structural/functional role of the dimeric structure in Cu,Zn superoxide dismutases, we have studied the stability to a variety of agents of the Escherichia coli enzyme, the only monomeric variant of this class so far isolated. Differential scanning calorimetry of the native enzyme showed the presence of two well defined peaks identified as the metal free and holoprotein. Unlike dimeric Cu,Zn superoxide dismutases, the unfolding of the monomeric enzyme was found to be highly… CONTINUE READING

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