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    Por favor, use este identificador para citar o enlazar este ítem: http://hdl.handle.net/10259/4766

    Título
    Structure and function of Aspergillus niger laccase McoG
    Autor
    Ferraroni, Marta .
    Westphal, Adrie H. .
    Borsari, Marco .
    Tamayo Ramos, Juan AntonioAutoridad UBU Orcid
    Briganti, Fabrizio .
    Graaff, Leo H. de .
    Berkel, Willem J. H. van .
    Publicado en
    Biocatalysis. 2017, V. 3, n.1, p. 1-16
    Editorial
    De Gruyter
    Fecha de publicación
    2017-01
    ISSN
    2353-1746
    DOI
    10.1515/boca-2017-0001
    Zusammenfassung
    The ascomycete Aspergillus niger produces several multicopper oxidases, but their biocatalytic properties remain largely unknown. Elucidation of the crystal structure of A. niger laccase McoG at 1.7 Å resolution revealed that the C-terminal tail of this glycoprotein blocks the T3 solvent channel and that a peroxide ion bridges the two T3 copper atoms. Remarkably, McoG contains a histidine (His253) instead of the common aspartate or glutamate expected to be involved in catalytic proton transfer with phenolic compounds. The crystal structure of H253D at 1.5 Å resolution resembles the wild type structure. McoG and the H253D, H253A and H253N variants have similar activities with 2,2’-azino-bis(3- ethylbenzothiazoline-6-sulphonic acid or N,N-dimethyl-p-phenylenediamine sulphate. However, the activities of H253A and H253N with 2-amino-4-methylphenol and 2-amino-4-methoxyphenol are strongly reduced compared to that of wild type. The redox potentials and electron transfer rates (ks) of wild type and variants were determined (McoG wt E°’ is +453 mV), and especially the reduced ks values of H253A and H253N show strong correlation with their low activity on phenolic compounds. In summary, our results suggest that the His253 adaptation of McoG can be beneficial for the conversion of phenolic compounds.
    Palabras clave
    Aspergillus niger
    crystal structure
    laccase
    redox potential
    metalloprotein
    multicopper oxidase
    Materia
    Química física
    Chemistry, Physical and theoretical
    URI
    http://hdl.handle.net/10259/4766
    Versión del editor
    https://doi.org/10.1515/boca-2017-0001
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    Attribution-NonCommercial-NoDerivs 3.0 Unported
    Documento(s) sujeto(s) a una licencia Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported
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    Ferraroni-Biocatalysis_2017.pdf
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