Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant

11p.-5 fig.-1 tab. + 13 p.- Supporting Information

Detalles Bibliográficos
Autores: Houtman, Carl J., Maligaspe, Eranda, Hunt, Christopher G., Fernández-Fueyo, Elena, Martínez, Ángel T., Hammel, Kenneth E.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2018
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/163821
Acceso en línea:http://hdl.handle.net/10261/163821
Access Level:acceso abierto
Palabra clave:Phanerochaete chrysosporium
Biodegradation
Computer modeling
Confocal microscopy
Free radicals
Imaging
Lignin degradation
Peroxidase
White rot fungus
id ES_1d6e5eed2edfbc8f503b2b9a5d9eba97
oai_identifier_str oai:digital.csic.es:10261/163821
network_acronym_str ES
network_name_str España
repository_id_str
spelling Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidantHoutman, Carl J.Maligaspe, ErandaHunt, Christopher G.Fernández-Fueyo, ElenaMartínez, Ángel T.Hammel, Kenneth E.Phanerochaete chrysosporiumBiodegradationComputer modelingConfocal microscopyFree radicalsImagingLignin degradationPeroxidaseWhite rot fungus11p.-5 fig.-1 tab. + 13 p.- Supporting InformationPeroxidases are considered essential agents of lignin degradation by white-rot basidiomycetes. However, low-molecular-weight oxidants likely have a primary role in lignin breakdown because many of these fungi delignify wood before its porosity has sufficiently increased for enzymes to infiltrate. It has been proposed that lignin peroxidases (LPs, EC 1.11.1.14) fulfill this role by oxidizing the secreted fungal metabolite veratryl alcohol (VA) to its aryl cation radical (VA+•), releasing it to act as a one-electron lignin oxidant within woody plant cell walls. Here, we attached the fluorescent oxidant sensor BODIPY 581/591 throughout beads with a nominal porosity of 6 kDa and assessed whether peroxidase-generated aryl cation radical systems could oxidize the beads. As positive control, we used the 1,2,4,5-tetramethoxybenzene (TMB) cation radical, generated from TMB by horseradish peroxidase. This control oxidized the beads to depths that increased with the amount of oxidant supplied, ultimately resulting in completely oxidized beads. A reaction-diffusion computer model yielded oxidation profiles that were within the 95% confidence intervals for the data. By contrast, bead oxidation caused by VA and the LPA isozyme of Phanerochaete chrysosporium was confined to a shallow shell of LP-accessible volume at the bead surface, regardless of how much oxidant was supplied. This finding contrasted with the modeling results, which showed that if the LP/VA system were to release VA+•, it would oxidize the bead interiors. We conclude that LPA releases insignificant quantities of VA+• and that a different mechanism produces small ligninolytic oxidants during white rot.This work was supported by United States Department of Energy, Office of Biological and Environmental Research Grant DE-SC0006929 (to K. E. H.,C. J. H.,and C. G. H.)Peer reviewedAmerican Society for Biochemistry and Molecular BiologyBiological and Environmental Research (US)Department of Energy (US)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201820182018info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/163821reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1074/jbc.RA117.001153Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1638212026-05-22T06:33:51Z
dc.title.none.fl_str_mv Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
title Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
spellingShingle Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
Houtman, Carl J.
Phanerochaete chrysosporium
Biodegradation
Computer modeling
Confocal microscopy
Free radicals
Imaging
Lignin degradation
Peroxidase
White rot fungus
title_short Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
title_full Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
title_fullStr Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
title_full_unstemmed Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
title_sort Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
dc.creator.none.fl_str_mv Houtman, Carl J.
Maligaspe, Eranda
Hunt, Christopher G.
Fernández-Fueyo, Elena
Martínez, Ángel T.
Hammel, Kenneth E.
author Houtman, Carl J.
author_facet Houtman, Carl J.
Maligaspe, Eranda
Hunt, Christopher G.
Fernández-Fueyo, Elena
Martínez, Ángel T.
Hammel, Kenneth E.
author_role author
author2 Maligaspe, Eranda
Hunt, Christopher G.
Fernández-Fueyo, Elena
Martínez, Ángel T.
Hammel, Kenneth E.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Biological and Environmental Research (US)
Department of Energy (US)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Phanerochaete chrysosporium
Biodegradation
Computer modeling
Confocal microscopy
Free radicals
Imaging
Lignin degradation
Peroxidase
White rot fungus
topic Phanerochaete chrysosporium
Biodegradation
Computer modeling
Confocal microscopy
Free radicals
Imaging
Lignin degradation
Peroxidase
White rot fungus
description 11p.-5 fig.-1 tab. + 13 p.- Supporting Information
publishDate 2018
dc.date.none.fl_str_mv 2018
2018
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/163821
url http://hdl.handle.net/10261/163821
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1074/jbc.RA117.001153
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869404279321657344
score 15,81155

Similares en LA Referencia