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|Title:||Tyrosyl Radical in the W164Y Mutant of P. eryngiiVersatile Peroxidase: an EPR and DFT/PCM Study||Authors:||Bernini, Caterina
|Issue Date:||2010||Project:||None||Journal:||APPLIED MAGNETIC RESONANCE||Abstract:||
Versatile peroxidases (VP) constitute a new class of high redox potentialfungal enzymes that are able to degrade lignin and large substrate molecules. Theseenzymes catalyze the oxidation of substrates at an exposed tryptophan radical formedby a long-range electron transfer mechanism to heme following the activation byH2O2.In a previous paper, it was demonstrated using electron paramagnetic resonance (EPR)and electron-nuclear double resonance experiments on wild-type VP that Trp164 wasthe radical site and that it was in a hydrogen-bonded neutral form. In this paper, theW164Y variant is analyzed and it is shown that also the variant is able to form the socalledCompound I (VPI) in the form of protein radical, although in different yieldswith respect to the wild type. The X-band EPR experiments in combination withdensity functional theory/polarizable continuum model calculations show that theW164Y mutant is able to form a neutral radical on Tyr164 residue, after activation byH2O2, but in contrast to Trp164, tyrosine is not expected to be hydrogen bonded.
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