Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/10249
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dc.contributor.authorRuiz-Dueñas, F. J.-
dc.contributor.authorMorales, María-
dc.contributor.authorGarcía-Ruiz, Eva-
dc.contributor.authorMiki, Yuta-
dc.contributor.authorMartínez, María Jesús-
dc.contributor.authorMartínez, Ángel T.-
dc.date.issued2008-11-05-
dc.identifier.citationJournal of Experimental Botany 60 (2) :441-52 (2009)en_US
dc.identifier.issn0022-0957-
dc.identifier.urihttp://hdl.handle.net/10261/10249-
dc.description12 pages, 2 figures.-- PMID: 18987391 PubMeden_US
dc.description.abstractVersatile peroxidase (VP) is defined by its capabilities to oxidize the typical substrates of other basidiomycete peroxidases: (i) Mn(2+), the manganese peroxidase (MnP) substrate (Mn(3+) being able to oxidize phenols and initiate lipid peroxidation reactions); (ii) veratryl alcohol (VA), the typical lignin peroxidase (LiP) substrate; and (iii) simple phenols, which are the substrates of Coprinopsis cinerea peroxidase (CIP). Crystallographic, spectroscopic, directed mutagenesis, and kinetic studies showed that these 'hybrid' properties are due to the coexistence in a single protein of different catalytic sites reminiscent of those present in the other basidiomycete peroxidase families. Crystal structures of wild and recombinant VP, and kinetics of mutated variants, revealed certain differences in its Mn-oxidation site compared with MnP. These result in efficient Mn(2+) oxidation in the presence of only two of the three acidic residues forming its binding site. On the other hand, a solvent-exposed tryptophan is the catalytically-active residue in VA oxidation, initiating an electron transfer pathway to haem (two other putative pathways were discarded by mutagenesis). Formation of a tryptophanyl radical after VP activation by peroxide was detected using electron paramagnetic resonance. This was the first time that a protein radical was directly demonstrated in a ligninolytic peroxidase. In contrast with LiP, the VP catalytic tryptophan is not beta-hydroxylated under hydrogen peroxide excess. It was also shown that the tryptophan environment affected catalysis, its modification introducing some LiP properties in VP. Moreover, some phenols and dyes are oxidized by VP at the edge of the main haem access channel, as found in CIP. Finally, the biotechnological interest of VP is discussed.en_US
dc.description.sponsorshipThis work was supported by the Spanish project BIO2005-03569 and BIO2008-01533, and the BIORENEW EU-project (NMP2-CT-2006-026456). The authors thank Klaus Piontek (Albert-Ludwigs University of Freiburg, Germany), María J Mate (CIB, CSIC, Madrid), and Antonio Romero (CIB, CSIC, Madrid) for crystallographic data; Rebecca Pogni and Riccardo Basosi (University of Sienna, Italy) for EPR analyses; and Andrew T Smith (University of Sussex, Brighton, UK) for helpful comments. FJR-D, EG, and YM thank the EU for a project contract, and MM thanks CSIC for an I3P fellowship.en_US
dc.language.isoengen_US
dc.publisherOxford University Pressen_US
dc.rightsopenAccessen_US
dc.subjectCrystal structuresen_US
dc.subjectFungal peroxidasesen_US
dc.subjectHaem access-channelen_US
dc.subjectLignin biodegradationen_US
dc.subjectManganese-binding siteen_US
dc.subjectSite-directed mutagenesisen_US
dc.subjectSpectroscopic analysesen_US
dc.subjectTransient-state kineticsen_US
dc.subjectTryptophanyl radicalen_US
dc.subjectVersatile peroxidaseen_US
dc.titleSubstrate oxidation sites in versatile peroxidase and other basidiomycete peroxidasesen_US
dc.typeartículoen_US
dc.identifier.doi10.1093/jxb/ern261-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://dx.doi.org/10.1093/jxb/ern261en_US
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item.openairetypeartículo-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.grantfulltextopen-
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