Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation?
Identifieur interne : 000A88 ( Main/Corpus ); précédent : 000A87; suivant : 000A89Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation?
Auteurs : L. Hildén ; G. Johansson ; G. Pettersson ; J. Li ; P. Ljungquist ; G. HenrikssonSource :
- FEBS letters [ 0014-5793 ] ; 2000.
English descriptors
- KwdEn :
- Anisoles (chemistry), Anisoles (metabolism), Benzyl Alcohols (chemistry), Benzyl Alcohols (metabolism), Biodegradation, Environmental (MeSH), Carbohydrate Dehydrogenases (metabolism), Chromatography, High Pressure Liquid (MeSH), Gas Chromatography-Mass Spectrometry (MeSH), Glycols (chemistry), Glycols (metabolism), Hydrogen Peroxide (metabolism), Hydroxyl Radical (metabolism), Hydroxylation (MeSH), Lignin (chemistry), Lignin (metabolism), Manganese Compounds (metabolism), Oxidants (metabolism), Oxidation-Reduction (MeSH), Peroxidases (metabolism), Phanerochaete (enzymology), Phenols (metabolism), Spectrophotometry, Ultraviolet (MeSH).
- MESH :
- chemical , chemistry : Anisoles, Benzyl Alcohols, Glycols, Lignin.
- chemical , metabolism : Anisoles, Benzyl Alcohols, Carbohydrate Dehydrogenases, Glycols, Hydrogen Peroxide, Hydroxyl Radical, Lignin, Manganese Compounds, Oxidants, Peroxidases, Phenols.
- enzymology : Phanerochaete.
- Biodegradation, Environmental, Chromatography, High Pressure Liquid, Gas Chromatography-Mass Spectrometry, Hydroxylation, Oxidation-Reduction, Spectrophotometry, Ultraviolet.
Abstract
The extracellular enzyme manganese peroxidase is believed to degrade lignin by a hydrogen peroxide-dependent oxidation of Mn(II) to the reactive species Mn(III) that attacks the lignin. However, Mn(III) is not able to directly oxidise the non-phenolic lignin structures that predominate in native lignin. We show here that pretreatment of a non-phenolic lignin model compound with another extracellular fungal enzyme, cellobiose dehydrogenase, allows the manganese peroxidase system to oxidise this molecule. The mechanism behind this effect is demethoxylation and/or hydroxylation, i.e. conversion of a non-phenolic structure to a phenolic one, mediated by hydroxyl radicals generated by cellobiose dehydrogenase. This suggests that cellobiose dehydrogenase and manganese peroxidase may act in an extracellular pathway in fungal lignin biodegradation. Analytical techniques used in this paper are reverse-phase high-pressure liquid chromatography, gas chromatography connected to mass spectroscopy and UV-visible spectroscopy.
DOI: 10.1016/s0014-5793(00)01757-9
PubMed: 10899314
Links to Exploration step
pubmed:10899314Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation?</title><author><name sortKey="Hilden, L" sort="Hilden, L" uniqKey="Hilden L" first="L" last="Hildén">L. Hildén</name><affiliation><nlm:affiliation>Department of Pulp and Paper Chemistry and Technology, Royal Institute of Technology, Drottning Kristinas väg 53, SE-100 44 Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Johansson, G" sort="Johansson, G" uniqKey="Johansson G" first="G" last="Johansson">G. Johansson</name></author><author><name sortKey="Pettersson, G" sort="Pettersson, G" uniqKey="Pettersson G" first="G" last="Pettersson">G. Pettersson</name></author><author><name sortKey="Li, J" sort="Li, J" uniqKey="Li J" first="J" last="Li">J. Li</name></author><author><name sortKey="Ljungquist, P" sort="Ljungquist, P" uniqKey="Ljungquist P" first="P" last="Ljungquist">P. Ljungquist</name></author><author><name sortKey="Henriksson, G" sort="Henriksson, G" uniqKey="Henriksson G" first="G" last="Henriksson">G. Henriksson</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:10899314</idno><idno type="pmid">10899314</idno><idno type="doi">10.1016/s0014-5793(00)01757-9</idno><idno type="wicri:Area/Main/Corpus">000A88</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000A88</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation?</title><author><name sortKey="Hilden, L" sort="Hilden, L" uniqKey="Hilden L" first="L" last="Hildén">L. Hildén</name><affiliation><nlm:affiliation>Department of Pulp and Paper Chemistry and Technology, Royal Institute of Technology, Drottning Kristinas väg 53, SE-100 44 Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Johansson, G" sort="Johansson, G" uniqKey="Johansson G" first="G" last="Johansson">G. Johansson</name></author><author><name sortKey="Pettersson, G" sort="Pettersson, G" uniqKey="Pettersson G" first="G" last="Pettersson">G. Pettersson</name></author><author><name sortKey="Li, J" sort="Li, J" uniqKey="Li J" first="J" last="Li">J. Li</name></author><author><name sortKey="Ljungquist, P" sort="Ljungquist, P" uniqKey="Ljungquist P" first="P" last="Ljungquist">P. Ljungquist</name></author><author><name sortKey="Henriksson, G" sort="Henriksson, G" uniqKey="Henriksson G" first="G" last="Henriksson">G. Henriksson</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anisoles (chemistry)</term><term>Anisoles (metabolism)</term><term>Benzyl Alcohols (chemistry)</term><term>Benzyl Alcohols (metabolism)</term><term>Biodegradation, Environmental (MeSH)</term><term>Carbohydrate Dehydrogenases (metabolism)</term><term>Chromatography, High Pressure Liquid (MeSH)</term><term>Gas Chromatography-Mass Spectrometry (MeSH)</term><term>Glycols (chemistry)</term><term>Glycols (metabolism)</term><term>Hydrogen Peroxide (metabolism)</term><term>Hydroxyl Radical (metabolism)</term><term>Hydroxylation (MeSH)</term><term>Lignin (chemistry)</term><term>Lignin (metabolism)</term><term>Manganese Compounds (metabolism)</term><term>Oxidants (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Phenols (metabolism)</term><term>Spectrophotometry, Ultraviolet (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Anisoles</term><term>Benzyl Alcohols</term><term>Glycols</term><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Anisoles</term><term>Benzyl Alcohols</term><term>Carbohydrate Dehydrogenases</term><term>Glycols</term><term>Hydrogen Peroxide</term><term>Hydroxyl Radical</term><term>Lignin</term><term>Manganese Compounds</term><term>Oxidants</term><term>Peroxidases</term><term>Phenols</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Chromatography, High Pressure Liquid</term><term>Gas Chromatography-Mass Spectrometry</term><term>Hydroxylation</term><term>Oxidation-Reduction</term><term>Spectrophotometry, Ultraviolet</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The extracellular enzyme manganese peroxidase is believed to degrade lignin by a hydrogen peroxide-dependent oxidation of Mn(II) to the reactive species Mn(III) that attacks the lignin. However, Mn(III) is not able to directly oxidise the non-phenolic lignin structures that predominate in native lignin. We show here that pretreatment of a non-phenolic lignin model compound with another extracellular fungal enzyme, cellobiose dehydrogenase, allows the manganese peroxidase system to oxidise this molecule. The mechanism behind this effect is demethoxylation and/or hydroxylation, i.e. conversion of a non-phenolic structure to a phenolic one, mediated by hydroxyl radicals generated by cellobiose dehydrogenase. This suggests that cellobiose dehydrogenase and manganese peroxidase may act in an extracellular pathway in fungal lignin biodegradation. Analytical techniques used in this paper are reverse-phase high-pressure liquid chromatography, gas chromatography connected to mass spectroscopy and UV-visible spectroscopy.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10899314</PMID><DateCompleted><Year>2000</Year><Month>08</Month><Day>10</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>477</Volume><Issue>1-2</Issue><PubDate><Year>2000</Year><Month>Jul</Month><Day>14</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation?</ArticleTitle><Pagination><MedlinePgn>79-83</MedlinePgn></Pagination><Abstract><AbstractText>The extracellular enzyme manganese peroxidase is believed to degrade lignin by a hydrogen peroxide-dependent oxidation of Mn(II) to the reactive species Mn(III) that attacks the lignin. However, Mn(III) is not able to directly oxidise the non-phenolic lignin structures that predominate in native lignin. We show here that pretreatment of a non-phenolic lignin model compound with another extracellular fungal enzyme, cellobiose dehydrogenase, allows the manganese peroxidase system to oxidise this molecule. The mechanism behind this effect is demethoxylation and/or hydroxylation, i.e. conversion of a non-phenolic structure to a phenolic one, mediated by hydroxyl radicals generated by cellobiose dehydrogenase. This suggests that cellobiose dehydrogenase and manganese peroxidase may act in an extracellular pathway in fungal lignin biodegradation. Analytical techniques used in this paper are reverse-phase high-pressure liquid chromatography, gas chromatography connected to mass spectroscopy and UV-visible spectroscopy.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hildén</LastName><ForeName>L</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Pulp and Paper Chemistry and Technology, Royal Institute of Technology, Drottning Kristinas väg 53, SE-100 44 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Johansson</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Pettersson</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Ljungquist</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Henriksson</LastName><ForeName>G</ForeName><Initials>G</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000840">Anisoles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006018">Glycols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017895">Manganese Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016877">Oxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010636">Phenols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C411733">methylsyringylalcohol</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C411732">veratryl glycol</NameOfSubstance></Chemical><Chemical><RegistryNumber>3352-57-6</RegistryNumber><NameOfSubstance UI="D017665">Hydroxyl Radical</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D002237">Carbohydrate Dehydrogenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.99.18</RegistryNumber><NameOfSubstance UI="C019859">cellobiose-quinone oxidoreductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>MB4T4A711H</RegistryNumber><NameOfSubstance UI="C042197">veratryl alcohol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000840" MajorTopicYN="N">Anisoles</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008401" MajorTopicYN="N">Gas Chromatography-Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006018" MajorTopicYN="N">Glycols</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017665" MajorTopicYN="N">Hydroxyl Radical</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006900" MajorTopicYN="N">Hydroxylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017895" MajorTopicYN="N">Manganese Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016877" MajorTopicYN="N">Oxidants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010636" MajorTopicYN="N">Phenols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013056" MajorTopicYN="N">Spectrophotometry, Ultraviolet</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>7</Month><Day>19</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2000</Year><Month>8</Month><Day>12</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>7</Month><Day>19</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10899314</ArticleId><ArticleId IdType="pii">S0014-5793(00)01757-9</ArticleId><ArticleId IdType="doi">10.1016/s0014-5793(00)01757-9</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000A88 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 000A88 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhanerochaeteV1
|flux= Main
|étape= Corpus
|type= RBID
|clé= pubmed:10899314
|texte= Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation?
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Corpus/RBID.i -Sk "pubmed:10899314" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |