A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase

  title={A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase},
  author={Ivano Bertini and Mario Piccioli and Maria Silvia Viezzoli and Choi Ying Chiu and G. T. Mullenbach},
  journal={European Biophysics Journal},
A mutated protein of human Cu(II)2Zn(II)2 SOD in which residues Phe50 and Gly51 at the dimer interface were substituted by Glu's, thus producing a monomeric species, has been characterized by electronic absorption spectroscopy, EPR, relaxivity and1H NMR techniques. Such substitutions and/or accompanying remodeling and exposure of the dimer interface to solvent, alter the geometry of the active site: increases in the axiality of the copper chromophore and the Cu-OH2 distance have been observed… CONTINUE READING
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