Free hydroxyl radical is not involved in an important reaction of lignin degradation by Phanerochaete chrysosporium Burds.
Identifieur interne : 001056 ( Main/Exploration ); précédent : 001055; suivant : 001057Free hydroxyl radical is not involved in an important reaction of lignin degradation by Phanerochaete chrysosporium Burds.
Auteurs : T K Kirk ; M D Mozuch ; M. TienSource :
- The Biochemical journal [ 0264-6021 ] ; 1985.
Descripteurs français
- KwdFr :
- Champignons (métabolisme), Composés du fer II (pharmacologie), Fer (pharmacologie), Lignine (métabolisme), Modèles chimiques (MeSH), Oxygénases (pharmacologie), Peroxyde d'hydrogène (pharmacologie), Radicaux libres (MeSH), Spectrométrie de masse (MeSH), Spectroscopie de résonance de spin électronique (MeSH).
- MESH :
- métabolisme : Champignons, Lignine.
- pharmacologie : Composés du fer II, Fer, Oxygénases, Peroxyde d'hydrogène.
- Modèles chimiques, Radicaux libres, Spectrométrie de masse, Spectroscopie de résonance de spin électronique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Lignin.
- chemical , pharmacology : Ferrous Compounds, Hydrogen Peroxide, Iron, Oxygenases.
- metabolism : Fungi.
- Electron Spin Resonance Spectroscopy, Free Radicals, Mass Spectrometry, Models, Chemical.
Abstract
Hydroxyl radical (HO.) has been implicated in the degradation of lignin by Phanerochaete chrysosporium. This study assessed the possible involvement of HO. in degradation of lignin substructural models by intact cultures and by an extracellular ligninase isolated from the cultures. Two non-phenolic lignin model compounds [aryl-C(alpha)HOH-C(beta)HR-C(gamma)H2OH, in which R = aryl (beta-1) or R = O-aryl (beta-O-4)] were degraded by cultures, by the purified ligninase, and by Fenton's reagent (H2O2 + Fe2+), which generates HO.. The ligninase and the cultures formed similar products, derived via an initial cleavage between C(alpha) and C(beta) (known to be an important biodegradative reaction), indicating that the ligninase is responsible for model degradation in cultures. Products from the Fenton degradation were mainly polar phenolics that exhibited little similarity to those from the biological systems. Mass-spectral analysis, however, revealed traces of the same products in the Fenton reaction as seen in the biological reactions; even so, an 18O2-incorporation study showed that the mechanism of formation differed. E.s.r. spectroscopy with a spin-trapping agent readily detected HO. in the Fenton system, but indicated that no HO. is formed during ligninase catalysis. We conclude, therefore that HO. is not involved in fungal C(alpha)-C(beta) cleavage in the beta-1 and beta-O-4 models and, by extension, in the same reaction in lignin.
DOI: 10.1042/bj2260455
PubMed: 2986597
PubMed Central: PMC1144732
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Free hydroxyl radical is not involved in an important reaction of lignin degradation by Phanerochaete chrysosporium Burds.</title><author><name sortKey="Kirk, T K" sort="Kirk, T K" uniqKey="Kirk T" first="T K" last="Kirk">T K Kirk</name></author><author><name sortKey="Mozuch, M D" sort="Mozuch, M D" uniqKey="Mozuch M" first="M D" last="Mozuch">M D Mozuch</name></author><author><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1985">1985</date><idno type="RBID">pubmed:2986597</idno><idno type="pmid">2986597</idno><idno type="pmc">PMC1144732</idno><idno type="doi">10.1042/bj2260455</idno><idno type="wicri:Area/Main/Corpus">001058</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001058</idno><idno type="wicri:Area/Main/Curation">001058</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001058</idno><idno type="wicri:Area/Main/Exploration">001058</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Free hydroxyl radical is not involved in an important reaction of lignin degradation by Phanerochaete chrysosporium Burds.</title><author><name sortKey="Kirk, T K" sort="Kirk, T K" uniqKey="Kirk T" first="T K" last="Kirk">T K Kirk</name></author><author><name sortKey="Mozuch, M D" sort="Mozuch, M D" uniqKey="Mozuch M" first="M D" last="Mozuch">M D Mozuch</name></author><author><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="ISSN">0264-6021</idno><imprint><date when="1985" type="published">1985</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Ferrous Compounds (pharmacology)</term><term>Free Radicals (MeSH)</term><term>Fungi (metabolism)</term><term>Hydrogen Peroxide (pharmacology)</term><term>Iron (pharmacology)</term><term>Lignin (metabolism)</term><term>Mass Spectrometry (MeSH)</term><term>Models, Chemical (MeSH)</term><term>Oxygenases (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Champignons (métabolisme)</term><term>Composés du fer II (pharmacologie)</term><term>Fer (pharmacologie)</term><term>Lignine (métabolisme)</term><term>Modèles chimiques (MeSH)</term><term>Oxygénases (pharmacologie)</term><term>Peroxyde d'hydrogène (pharmacologie)</term><term>Radicaux libres (MeSH)</term><term>Spectrométrie de masse (MeSH)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Ferrous Compounds</term><term>Hydrogen Peroxide</term><term>Iron</term><term>Oxygenases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Champignons</term><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Composés du fer II</term><term>Fer</term><term>Oxygénases</term><term>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Spin Resonance Spectroscopy</term><term>Free Radicals</term><term>Mass Spectrometry</term><term>Models, Chemical</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Modèles chimiques</term><term>Radicaux libres</term><term>Spectrométrie de masse</term><term>Spectroscopie de résonance de spin électronique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Hydroxyl radical (HO.) has been implicated in the degradation of lignin by Phanerochaete chrysosporium. This study assessed the possible involvement of HO. in degradation of lignin substructural models by intact cultures and by an extracellular ligninase isolated from the cultures. Two non-phenolic lignin model compounds [aryl-C(alpha)HOH-C(beta)HR-C(gamma)H2OH, in which R = aryl (beta-1) or R = O-aryl (beta-O-4)] were degraded by cultures, by the purified ligninase, and by Fenton's reagent (H2O2 + Fe2+), which generates HO.. The ligninase and the cultures formed similar products, derived via an initial cleavage between C(alpha) and C(beta) (known to be an important biodegradative reaction), indicating that the ligninase is responsible for model degradation in cultures. Products from the Fenton degradation were mainly polar phenolics that exhibited little similarity to those from the biological systems. Mass-spectral analysis, however, revealed traces of the same products in the Fenton reaction as seen in the biological reactions; even so, an 18O2-incorporation study showed that the mechanism of formation differed. E.s.r. spectroscopy with a spin-trapping agent readily detected HO. in the Fenton system, but indicated that no HO. is formed during ligninase catalysis. We conclude, therefore that HO. is not involved in fungal C(alpha)-C(beta) cleavage in the beta-1 and beta-O-4 models and, by extension, in the same reaction in lignin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2986597</PMID><DateCompleted><Year>1985</Year><Month>05</Month><Day>24</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0264-6021</ISSN><JournalIssue CitedMedium="Print"><Volume>226</Volume><Issue>2</Issue><PubDate><Year>1985</Year><Month>Mar</Month><Day>01</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Free hydroxyl radical is not involved in an important reaction of lignin degradation by Phanerochaete chrysosporium Burds.</ArticleTitle><Pagination><MedlinePgn>455-60</MedlinePgn></Pagination><Abstract><AbstractText>Hydroxyl radical (HO.) has been implicated in the degradation of lignin by Phanerochaete chrysosporium. This study assessed the possible involvement of HO. in degradation of lignin substructural models by intact cultures and by an extracellular ligninase isolated from the cultures. Two non-phenolic lignin model compounds [aryl-C(alpha)HOH-C(beta)HR-C(gamma)H2OH, in which R = aryl (beta-1) or R = O-aryl (beta-O-4)] were degraded by cultures, by the purified ligninase, and by Fenton's reagent (H2O2 + Fe2+), which generates HO.. The ligninase and the cultures formed similar products, derived via an initial cleavage between C(alpha) and C(beta) (known to be an important biodegradative reaction), indicating that the ligninase is responsible for model degradation in cultures. Products from the Fenton degradation were mainly polar phenolics that exhibited little similarity to those from the biological systems. Mass-spectral analysis, however, revealed traces of the same products in the Fenton reaction as seen in the biological reactions; even so, an 18O2-incorporation study showed that the mechanism of formation differed. E.s.r. spectroscopy with a spin-trapping agent readily detected HO. in the Fenton system, but indicated that no HO. is formed during ligninase catalysis. We conclude, therefore that HO. is not involved in fungal C(alpha)-C(beta) cleavage in the beta-1 and beta-O-4 models and, by extension, in the same reaction in lignin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kirk</LastName><ForeName>T K</ForeName><Initials>TK</Initials></Author><Author ValidYN="Y"><LastName>Mozuch</LastName><ForeName>M D</ForeName><Initials>MD</Initials></Author><Author ValidYN="Y"><LastName>Tien</LastName><ForeName>M</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C045076">Fenton's reagent</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005296">Ferrous Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005609">Free Radicals</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>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.13.-</RegistryNumber><NameOfSubstance UI="D010105">Oxygenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.99.-</RegistryNumber><NameOfSubstance UI="C044391">ligninase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005296" MajorTopicYN="N">Ferrous Compounds</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005609" MajorTopicYN="N">Free Radicals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010105" MajorTopicYN="N">Oxygenases</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1985</Year><Month>3</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1985</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1985</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2986597</ArticleId><ArticleId IdType="pmc">PMC1144732</ArticleId><ArticleId IdType="doi">10.1042/bj2260455</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 1983 Aug 12;114(3):1077-83</Citation><ArticleIdList><ArticleId IdType="pubmed">6615503</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1983 Nov;46(5):1140-5</Citation><ArticleIdList><ArticleId IdType="pubmed">16346420</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1984 Apr;81(8):2280-4</Citation><ArticleIdList><ArticleId IdType="pubmed">16593451</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1982 Oct 10;257(19):11455-62</Citation><ArticleIdList><ArticleId IdType="pubmed">6288685</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1983 Aug 12;221(4611):661-3</Citation><ArticleIdList><ArticleId IdType="pubmed">17787736</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1980 Mar;200(1):1-16</Citation><ArticleIdList><ArticleId IdType="pubmed">6244786</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochimie. 1983 Apr-May;65(4-5):283-9</Citation><ArticleIdList><ArticleId IdType="pubmed">6409163</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1975 Jul;72(7):2515-9</Citation><ArticleIdList><ArticleId IdType="pubmed">1058470</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1982 Aug 15;206(2):423-5</Citation><ArticleIdList><ArticleId IdType="pubmed">7150253</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Biophys Res Commun. 1982 Nov 30;109(2):320-7</Citation><ArticleIdList><ArticleId IdType="pubmed">6295392</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Kirk, T K" sort="Kirk, T K" uniqKey="Kirk T" first="T K" last="Kirk">T K Kirk</name><name sortKey="Mozuch, M D" sort="Mozuch, M D" uniqKey="Mozuch M" first="M D" last="Mozuch">M D Mozuch</name><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001056 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001056 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhanerochaeteV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:2986597
|texte= Free hydroxyl radical is not involved in an important reaction of lignin degradation by Phanerochaete chrysosporium Burds.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:2986597" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |