Catalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study

@inproceedings{Linde2015CatalyticSR,
  title={Catalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study},
  author={D. von der Linde and Rebecca Pogni and Marina Ca{\~n}ellas and F{\'a}tima Lucas and V{\'i}ctor Guallar and Maria Camilla Baratto and Adalgisa Sinicropi and Ver{\'o}nica S{\'a}ez-Jim{\'e}nez and Cristina Coscol{\'i}n and Antonio Romero and Francisco Javier Enr{\'i}quez Medrano and Francisco Javier Ruiz-Due{\~n}as and {\'A}ngel T Martinez},
  booktitle={The Biochemical journal},
  year={2015}
}
Dye-decolorizing peroxidase (DyP) of Auricularia auricula-judae has been expressed in Escherichia coli as a representative of a new DyP family, and subjected to mutagenic, spectroscopic, crystallographic and computational studies. The crystal structure of DyP shows a buried haem cofactor, and surface tryptophan and tyrosine residues potentially involved in long-range electron transfer from bulky dyes. Simulations using PELE (Protein Energy Landscape Exploration) software provided several… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 13 CITATIONS

References

Publications referenced by this paper.
SHOWING 1-10 OF 56 REFERENCES

Phenol oxidation by DyP-type peroxidases in comparison to fungal and plant peroxidases

  • C. Liers, E. Aranda, +5 authors M. Hofrichter
  • J. Mol. Catal. B Enzym
  • 2014

Similar Papers

Loading similar papers…