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. 2019 Jun 15:668:23-28.
doi: 10.1016/j.abb.2019.05.010. Epub 2019 May 13.

Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan

Dolores Linde  1 , Iván Ayuso-Fernández  1 , Francisco J Ruiz-Dueñas  1 , Angel T Martínez  2
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Free article

Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan

Dolores Linde et al. Arch Biochem Biophys. .
Free article

Abstract

Dye-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).

Keywords: Catalytic tryptophan; Dye-decolorizing peroxidase (DyP); Heme peroxidases; Long-range electron transfer (LRET); Nitrophenols; Versatile peroxidase (VP).

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