Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases

Combining 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...

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Autores: Acebes, Sandra, Ruiz-Dueñas, Francisco J., Toubes, Mario, Sáez-Jiménez, Veronica, Pérez-Boada, Marta, Lucas, M. Fatima, Martínez, Angel T., Guallar, Víctor|||0000-0002-4580-1114
Tipo de recurso: artículo
Fecha de publicación:2017
País:España
Institución:Universitat Politècnica de Catalunya (UPC)
Repositorio:UPCommons. Portal del coneixement obert de la UPC
Idioma:inglés
OAI Identifier:oai:upcommons.upc.edu:2117/106854
Acceso en línea:https://hdl.handle.net/2117/106854
https://dx.doi.org/10.1021/acs.jpcb.7b00835
Access Level:acceso abierto
Palabra clave:Enzyme complexes
Peroxidases
Enzymes
Enzims
Peròxids
Àrees temàtiques de la UPC::Enginyeria biomèdica
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spelling Mapping the Long-Range Electron Transfer Route in Ligninolytic PeroxidasesAcebes, SandraRuiz-Dueñas, Francisco J.Toubes, MarioSáez-Jiménez, VeronicaPérez-Boada, MartaLucas, M. FatimaMartínez, Angel T.Guallar, Víctor|||0000-0002-4580-1114Enzyme complexesPeroxidasesPeroxidasesEnzymesEnzimsPeròxidsÀrees temàtiques de la UPC::Enginyeria biomèdicaCombining 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.This 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.Peer ReviewedACS Publications20172017-04-0420172017-07-26journal articlehttp://purl.org/coar/resource_type/c_6501AMhttp://purl.org/coar/version/c_ab4af688f83e57aainfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/2117/106854https://dx.doi.org/10.1021/acs.jpcb.7b00835reponame:UPCommons. Portal del coneixement obert de la UPCinstname:Universitat Politècnica de Catalunya (UPC)InglésengEuropean Commission http://doi.org/10.13039/100010661 Horizon 2020 Framework Programme 720297 New enzymatic oxidation%2Foxyfunctionalization technologies for added value bio-based productsMinisterio de Economía y Competitividad http://doi.org/10.13039/501100003329 BIO2014-56388-R NUEVAS ENZIMAS OXIDATIVAS PARA UNA INDUSTRIA SOSTENIBLEopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:upcommons.upc.edu:2117/1068542026-05-27T15:37:01Z
dc.title.none.fl_str_mv Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
title Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
spellingShingle Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
Acebes, Sandra
Enzyme complexes
Peroxidases
Peroxidases
Enzymes
Enzims
Peròxids
Àrees temàtiques de la UPC::Enginyeria biomèdica
title_short Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
title_full Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
title_fullStr Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
title_full_unstemmed Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
title_sort Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
dc.creator.none.fl_str_mv Acebes, Sandra
Ruiz-Dueñas, Francisco J.
Toubes, Mario
Sáez-Jiménez, Veronica
Pérez-Boada, Marta
Lucas, M. Fatima
Martínez, Angel T.
Guallar, Víctor|||0000-0002-4580-1114
author Acebes, Sandra
author_facet Acebes, Sandra
Ruiz-Dueñas, Francisco J.
Toubes, Mario
Sáez-Jiménez, Veronica
Pérez-Boada, Marta
Lucas, M. Fatima
Martínez, Angel T.
Guallar, Víctor|||0000-0002-4580-1114
author_role author
author2 Ruiz-Dueñas, Francisco J.
Toubes, Mario
Sáez-Jiménez, Veronica
Pérez-Boada, Marta
Lucas, M. Fatima
Martínez, Angel T.
Guallar, Víctor|||0000-0002-4580-1114
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Enzyme complexes
Peroxidases
Peroxidases
Enzymes
Enzims
Peròxids
Àrees temàtiques de la UPC::Enginyeria biomèdica
topic Enzyme complexes
Peroxidases
Peroxidases
Enzymes
Enzims
Peròxids
Àrees temàtiques de la UPC::Enginyeria biomèdica
description Combining 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.
publishDate 2017
dc.date.none.fl_str_mv 2017
2017-04-04
2017
2017-07-26
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
AM
http://purl.org/coar/version/c_ab4af688f83e57aa
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/2117/106854
https://dx.doi.org/10.1021/acs.jpcb.7b00835
url https://hdl.handle.net/2117/106854
https://dx.doi.org/10.1021/acs.jpcb.7b00835
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv European Commission http://doi.org/10.13039/100010661 Horizon 2020 Framework Programme 720297 New enzymatic oxidation%2Foxyfunctionalization technologies for added value bio-based products
Ministerio de Economía y Competitividad http://doi.org/10.13039/501100003329 BIO2014-56388-R NUEVAS ENZIMAS OXIDATIVAS PARA UNA INDUSTRIA SOSTENIBLE
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv ACS Publications
publisher.none.fl_str_mv ACS Publications
dc.source.none.fl_str_mv reponame:UPCommons. Portal del coneixement obert de la UPC
instname:Universitat Politècnica de Catalunya (UPC)
instname_str Universitat Politècnica de Catalunya (UPC)
reponame_str UPCommons. Portal del coneixement obert de la UPC
collection UPCommons. Portal del coneixement obert de la UPC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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