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dc.contributor.authorFerraroni, Marta .
dc.contributor.authorWestphal, Adrie H. .
dc.contributor.authorBorsari, Marco .
dc.contributor.authorTamayo Ramos, Juan Antonio 
dc.contributor.authorBriganti, Fabrizio .
dc.contributor.authorGraaff, Leo H. de .
dc.contributor.authorBerkel, Willem J. H. van .
dc.date.accessioned2018-03-22T08:44:59Z
dc.date.available2018-03-22T08:44:59Z
dc.date.issued2017-01
dc.identifier.issn2353-1746
dc.identifier.urihttp://hdl.handle.net/10259/4766
dc.description.abstractThe 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.en
dc.format.mimetypeapplication/pdf
dc.language.isoenges
dc.publisherDe Gruyteren
dc.relation.ispartofBiocatalysis. 2017, V. 3, n.1, p. 1-16en
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Unported
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0
dc.subjectAspergillus nigeren
dc.subjectcrystal structureen
dc.subjectlaccaseen
dc.subjectredox potentialen
dc.subjectmetalloproteinen
dc.subjectmulticopper oxidaseen
dc.subject.otherQuímica físicaes
dc.subject.otherChemistry, Physical and theoreticalen
dc.titleStructure and function of Aspergillus niger laccase McoGen
dc.typeArtículoes
dc.typeinfo:eu-repo/semantics/article
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.relation.publisherversionhttps://doi.org/10.1515/boca-2017-0001
dc.identifier.doi10.1515/boca-2017-0001
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersionen


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