Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase.

@article{Smith2009SpectroscopicEF,
  title={Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase.},
  author={Andrew T. Smith and Wendy A Doyle and Pierre Dorlet and Anabella Ivancich},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 38},
  pages={16084-9}
}
The surface oxidation site (Trp-171) in lignin peroxidase (LiP) required for the reaction with veratryl alcohol a high-redox-potential (1.4 V) substrate, was engineered into Coprinus cinereus peroxidase (CiP) by introducing a Trp residue into a heme peroxidase that has similar protein fold but lacks this activity. To create the catalytic activity toward veratryl alcohol in CiP, it was necessary to reproduce the Trp site and its negatively charged microenvironment by means of a triple mutation… CONTINUE READING

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