Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant.
Identifieur interne : 000114 ( Main/Exploration ); précédent : 000113; suivant : 000115Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant.
Auteurs : Carl J. Houtman [États-Unis] ; Eranda Maligaspe [États-Unis] ; Christopher G. Hunt [États-Unis] ; Elena Fernández-Fueyo ; Angel T. Martínez ; Kenneth E. Hammel [États-Unis]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2018.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Alcools benzyliques, Peroxidases, Protéines fongiques, Radicaux libres.
- enzymologie : Polyporales.
- Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Benzyl Alcohols, Free Radicals, Fungal Proteins, Peroxidases.
- enzymology : Polyporales.
- Oxidation-Reduction.
Abstract
Peroxidases 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.
DOI: 10.1074/jbc.RA117.001153
PubMed: 29462790
PubMed Central: PMC5880153
Affiliations:
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Hammel</name><affiliation wicri:level="1"><nlm:affiliation>From the United States Forest Products Laboratory, Madison, Wisconsin 53726, kehammel@wisc.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>From the United States Forest Products Laboratory, Madison, Wisconsin 53726</wicri:regionArea><wicri:noRegion>Wisconsin 53726</wicri:noRegion></affiliation><affiliation wicri:level="2"><nlm:affiliation>the Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Wisconsin</region></placeName><wicri:cityArea>the Department of Bacteriology, University of Wisconsin, Madison</wicri:cityArea></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Benzyl Alcohols (chemistry)</term><term>Free Radicals (chemistry)</term><term>Fungal Proteins (chemistry)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Polyporales (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcools benzyliques (composition chimique)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (composition chimique)</term><term>Polyporales (enzymologie)</term><term>Protéines fongiques (composition chimique)</term><term>Radicaux libres (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Benzyl Alcohols</term><term>Free Radicals</term><term>Fungal Proteins</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Alcools benzyliques</term><term>Peroxidases</term><term>Protéines fongiques</term><term>Radicaux libres</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Polyporales</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Polyporales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Peroxidases 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<sup>+•</sup>), 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 <i>Phanerochaete chrysosporium</i> 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<sup>+•</sup>, it would oxidize the bead interiors. We conclude that LPA releases insignificant quantities of VA<sup>+•</sup> and that a different mechanism produces small ligninolytic oxidants during white rot.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29462790</PMID><DateCompleted><Year>2019</Year><Month>04</Month><Day>08</Day></DateCompleted><DateRevised><Year>2019</Year><Month>04</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>293</Volume><Issue>13</Issue><PubDate><Year>2018</Year><Month>03</Month><Day>30</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant.</ArticleTitle><Pagination><MedlinePgn>4702-4712</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA117.001153</ELocationID><Abstract><AbstractText>Peroxidases 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<sup>+•</sup>), 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 <i>Phanerochaete chrysosporium</i> 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<sup>+•</sup>, it would oxidize the bead interiors. We conclude that LPA releases insignificant quantities of VA<sup>+•</sup> and that a different mechanism produces small ligninolytic oxidants during white rot.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Houtman</LastName><ForeName>Carl J</ForeName><Initials>CJ</Initials><AffiliationInfo><Affiliation>From the United States Forest Products Laboratory, Madison, Wisconsin 53726.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Maligaspe</LastName><ForeName>Eranda</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>From the United States Forest Products Laboratory, Madison, Wisconsin 53726.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hunt</LastName><ForeName>Christopher G</ForeName><Initials>CG</Initials><AffiliationInfo><Affiliation>From the United States Forest Products Laboratory, Madison, Wisconsin 53726.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fernández-Fueyo</LastName><ForeName>Elena</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>the Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>Angel T</ForeName><Initials>AT</Initials><AffiliationInfo><Affiliation>the Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hammel</LastName><ForeName>Kenneth E</ForeName><Initials>KE</Initials><AffiliationInfo><Affiliation>From the United States Forest Products Laboratory, Madison, Wisconsin 53726, kehammel@wisc.edu.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>the Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>02</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005609">Free Radicals</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>MB4T4A711H</RegistryNumber><NameOfSubstance UI="C042197">veratryl alcohol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005609" MajorTopicYN="N">Free Radicals</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020072" MajorTopicYN="N">Polyporales</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Phanerochaete chrysosporium</Keyword><Keyword MajorTopicYN="Y">biodegradation</Keyword><Keyword MajorTopicYN="Y">computer modeling</Keyword><Keyword MajorTopicYN="Y">confocal microscopy</Keyword><Keyword MajorTopicYN="Y">free radicals</Keyword><Keyword MajorTopicYN="Y">imaging</Keyword><Keyword MajorTopicYN="Y">lignin degradation</Keyword><Keyword MajorTopicYN="Y">peroxidase</Keyword><Keyword MajorTopicYN="Y">white rot fungus</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate 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Martínez</name></noCountry><country name="États-Unis"><region name="Wisconsin"><name sortKey="Houtman, Carl J" sort="Houtman, Carl J" uniqKey="Houtman C" first="Carl J" last="Houtman">Carl J. Houtman</name></region><name sortKey="Hammel, Kenneth E" sort="Hammel, Kenneth E" uniqKey="Hammel K" first="Kenneth E" last="Hammel">Kenneth E. Hammel</name><name sortKey="Hammel, Kenneth E" sort="Hammel, Kenneth E" uniqKey="Hammel K" first="Kenneth E" last="Hammel">Kenneth E. Hammel</name><name sortKey="Hunt, Christopher G" sort="Hunt, Christopher G" uniqKey="Hunt C" first="Christopher G" last="Hunt">Christopher G. Hunt</name><name sortKey="Maligaspe, Eranda" sort="Maligaspe, Eranda" uniqKey="Maligaspe E" first="Eranda" last="Maligaspe">Eranda Maligaspe</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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