Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways.

@article{PrezBoada2005VersatilePO,
  title={Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways.},
  author={Marta P{\'e}rez-Boada and Francisco Javier Ruiz-Due{\~n}as and Rebecca Pogni and Riccardo Basosi and Thomas Choinowski and Mar{\'i}a Jes{\'u}s Mart{\'i}nez and Klaus Piontek and {\'A}ngel T Martinez},
  journal={Journal of molecular biology},
  year={2005},
  volume={354 2},
  pages={385-402}
}
Versatile peroxidases (VP), a recently described family of ligninolytic peroxidases, show a hybrid molecular architecture combining different oxidation sites connected to the heme cofactor. High-resolution crystal structures as well as homology models of VP isoenzymes from the fungus Pleurotus eryngii revealed three possibilities for long-range electron transfer for the oxidation of high redox potential aromatic compounds. The possible pathways would start either at Trp164 or His232 of… CONTINUE READING
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