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dc.contributor.authorAcebes, Sandra
dc.contributor.authorRuiz-Dueñas, Francisco J.
dc.contributor.authorToubes, Mario
dc.contributor.authorSáez-Jiménez, Veronica
dc.contributor.authorPérez-Boada, Marta
dc.contributor.authorLucas, M. Fatima
dc.contributor.authorMartínez, Angel T.
dc.contributor.authorGuallar, Victor
dc.contributor.otherBarcelona Supercomputing Center
dc.date.accessioned2017-07-26T10:02:40Z
dc.date.available2018-04-04T00:30:39Z
dc.date.issued2017-04-04
dc.identifier.citationAcebes, S. [et al.]. Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases. "Journal of Physical Chemistry B", 4 Abril 2017, vol. 121, núm. 16, p. 3946-3954.
dc.identifier.issn1520-6106
dc.identifier.urihttp://hdl.handle.net/2117/106854
dc.description.abstractCombining a computational analysis with site-directed mutagenesis, we have studied the long-range electron transfer pathway in versatile and lignin peroxidases, two enzymes of biotechnological interest that play a key role for fungal degradation of the bulky lignin molecule in plant biomass. The in silico study established two possible electron transfer routes starting at the surface tryptophan residue previously identified as responsible for oxidation of the bulky lignin polymer. Moreover, in both enzymes, a second buried tryptophan residue appears as a top electron transfer carrier, indicating the prevalence of one pathway. Site-directed mutagenesis of versatile peroxidase (from Pleurotus eryngii) allowed us to corroborate the computational analysis and the role played by the buried tryptophan (Trp244) and a neighbor phenylalanine residue (Phe198), together with the surface tryptophan, in the electron transfer. These three aromatic residues are highly conserved in all the sequences analyzed (up to a total of 169). The importance of the surface (Trp171) and buried (Trp251) tryptophan residues in lignin peroxidase has been also confirmed by directed mutagenesis of the Phanerochaete chrysosporium enzyme. Overall, the combined procedure identifies analogous electron transfer pathways in the long-range oxidation mechanism for both ligninolytic peroxidases, constituting a good example of how computational analysis avoids making extensive trial-error mutagenic experiments.
dc.description.sponsorshipThis work was supported by the INDOX (KBBE-2013-7-613549) EU project, and by the projects EnzOx2 (H2020-BBI-PPP-2015-2-720297) of the Joint Undertaking of European BioBased Industries (www.bbi-europe.eu), and BIO2014-56388-R (NOESIS) and CTQ2016-79138-R of the SpanishMinistry of Economy and Competitiveness (MINECO). F.J.R.-D. acknowledges a MINECO Ramón & Cajal contract.
dc.format.extent9 p.
dc.language.isoeng
dc.publisherACS Publications
dc.subjectÀrees temàtiques de la UPC::Enginyeria biomèdica
dc.subject.lcshEnzyme complexes
dc.subject.lcshPeroxidases
dc.subject.otherPeroxidases
dc.subject.otherEnzymes
dc.titleMapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
dc.typeArticle
dc.subject.lemacEnzims
dc.subject.lemacPeròxids
dc.identifier.doi10.1021/acs.jpcb.7b00835
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://pubs.acs.org/doi/abs/10.1021/acs.jpcb.7b00835
dc.rights.accessOpen Access
dc.description.versionPostprint (author's final draft)
dc.relation.projectidinfo:eu-repo/grantAgreement/EC/H2020/720297/EU/New enzymatic oxidation%2Foxyfunctionalization technologies for added value bio-based products/EnzOx2
dc.relation.projectidinfo:eu-repo/grantAgreement/MINECO/1PE/BIO2014-56388-R
dc.relation.projectidinfo:eu-repo/grantAgreement/MINECO/1PE/CTQ2016-79138-R
local.citation.publicationNameJournal of Physical Chemistry B
local.citation.volume121
local.citation.number16
local.citation.startingPage3946
local.citation.endingPage3954


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