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Título: | Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan |
Autor: | Linde, Dolores CSIC ORCID ; Ayuso-Fernández, Iván CSIC ORCID; Ruiz-Dueñas, F. J. CSIC ORCID ; Martínez, Ángel T. CSIC ORCID | Palabras clave: | Nitrophenols Heme peroxidases Long-range electron transfer (LRET) Catalytic tryptophan Dye-decolorizing peroxidase (DyP) Versatile peroxidase (VP) |
Fecha de publicación: | 15-jun-2019 | Editor: | Elsevier | Citación: | Archives of Biochemistry and Biophysics 668:23-28 (2019) | Resumen: | 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). | Descripción: | 21 p.-4 fig.-1 tab.-10 fig. supl.-2 tab. supl. | Versión del editor: | https://doi.org/10.1016/j.abb.2019.05.010 | URI: | http://hdl.handle.net/10261/181706 | DOI: | 10.1016/j.abb.2019.05.010 | ISSN: | 0003-9861 | E-ISSN: | 1096-0384 |
Aparece en las colecciones: | (CIB) Artículos |
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2019-Linde-ABB-accepted-manuscript-REVISED-1.pdf | 3,3 MB | Adobe PDF | Visualizar/Abrir |
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