Proximal mutations at the type 1 copper site of CotA laccase: spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants.

@article{Duro2008ProximalMA,
  title={Proximal mutations at the type 1 copper site of CotA laccase: spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants.},
  author={Paulo Dur{\~a}o and Zhenjia Chen and Catarina S. Silva and Cl{\'a}udio M. Soares and Manuela M Pereira and Smilja Todorovic and Peter Hildebrandt and Isabel Bento and Peter F. Lindley and L{\'i}gia O. Martins},
  journal={The Biochemical journal},
  year={2008},
  volume={412 2},
  pages={
          339-46
        }
}
In the present study the CotA laccase from Bacillus subtilis has been mutated at two hydrophobic residues in the vicinity of the type 1 copper site. The mutation of Leu(386) to an alanine residue appears to cause only very subtle alterations in the properties of the enzyme indicating minimal changes in the structure of the copper centres. However, the replacement of Ile(494) by an alanine residue leads to significant changes in the enzyme. Thus the major visible absorption band is upshifted by… CONTINUE READING

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