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Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan

AuthorsLinde, Dolores ; Ayuso-Fernández, Iván ; Ruiz-Dueñas, F. J. ; Martínez, Ángel T.
Heme peroxidases
Long-range electron transfer (LRET)
Catalytic tryptophan
Dye-decolorizing peroxidase (DyP)
Versatile peroxidase (VP)
Issue Date15-Jun-2019
CitationArchives of Biochemistry and Biophysics 668:23-28 (2019)
AbstractDye-decolorizing peroxidase (DyP) from Auricularia auricula-judae and versatile peroxidase (VP) from Pleurotus eryngii oxidize the three mononitrophenol isomers. Both enzymes have been overexpressed in Escherichia coli and in vitro activated. Despite their very different three-dimensional structures, the nitrophenol oxidation site is located at a solvent-exposed aromatic residue in both DyP (Trp377) and VP (Trp164), as revealed by liquid chromatography coupled to mass spectrometry and kinetic analyses of nitrophenol oxidation by the native enzymes and their tryptophan-less variants (the latter showing 10–60 fold lower catalytic efficiencies).
Description21 p.-4 fig.-1 tab.-10 fig. supl.-2 tab. supl.
Publisher version (URL)https://doi.org/10.1016/j.abb.2019.05.010
Appears in Collections:(CIB) Artículos
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