Ligninase of Phanerochaete chrysosporium. Mechanism of its degradation of the non-phenolic arylglycerol beta-aryl ether substructure of lignin.
Identifieur interne : 001038 ( Main/Exploration ); précédent : 001037; suivant : 001039Ligninase of Phanerochaete chrysosporium. Mechanism of its degradation of the non-phenolic arylglycerol beta-aryl ether substructure of lignin.
Auteurs : T K Kirk ; M. Tien ; P J Kersten ; M D Mozuch ; B. KalyanaramanSource :
- The Biochemical journal [ 0264-6021 ] ; 1986.
Descripteurs français
- KwdFr :
- MESH :
- analogues et dérivés : Lignine.
- enzymologie : Champignons.
- métabolisme : Lignine, Oxygénases.
- Modèles chimiques, Sites de fixation, Spectroscopie de résonance de spin électronique.
English descriptors
- KwdEn :
- MESH :
- chemical , analogs & derivatives : Lignin.
- enzymology : Fungi.
- chemical , metabolism : Lignin, Oxygenases.
- Binding Sites, Electron Spin Resonance Spectroscopy, Models, Chemical.
Abstract
This study examined the ligninase-catalysed degradation of lignin model compounds representing the arylglycerol beta-aryl ether substructure, which is the dominant one in the lignin polymer. Three dimeric model compounds were used, all methoxylated in the 3- and 4-positions of the arylglycerol ring (ring A) and having various substituents in the beta-ether-linked aromatic ring (ring B), so that competing reactions involving both rings could be compared. Studies of the products formed and the time courses of their formation showed that these model compounds are oxidized by ligninase (+ H2O2 + O2) in both ring A and ring B. The major consequence with all three model compounds is oxidation of ring A, leading primarily to cleavage between C(alpha) and C(beta) (C(alpha) being proximal to ring A), and to a lesser extent to the oxidation of the C(alpha)-hydroxy group to a carbonyl group. Such C(alpha)-oxidation deactivates ring A, leaving only ring B for attack. Studies with C(alpha)-carbonyl model compounds corresponding to the three basic model compounds revealed that oxidation of ring B leads in part to dealkoxylations (i.e. to cleavage of the glycerol beta-aryl ether bond and to demethoxylations), but that these are minor reactions in the model compounds most closely related to lignin. Evidence is also given that another consequence of oxidation of ring B in the C(alpha)-carbonyl model compounds is formation of unstable cyclohexadienone ketals, which can decompose with elimination of the beta-ether-linked aromatic ring. The mechanisms proposed for the observed reactions involve initial formation of aryl cation radicals in either ring A or ring B. The cation radical intermediate from one of the C(alpha)-carbonyl model compounds was identified by e.s.r. spectroscopy. The mechanisms are based on earlier studies showing that ligninase acts by oxidizing appropriately substituted aromatic nuclei to aryl cation radicals [Kersten, Tien, Kalyanaraman & Kirk (1985) J. Biol. Chem. 260, 2609-2612; Hammel, Tien, Kalyanaraman & Kirk (1985) J. Biol. Chem. 260, 8348-8353].
DOI: 10.1042/bj2360279
PubMed: 3024619
PubMed Central: PMC1146817
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Ligninase of Phanerochaete chrysosporium. Mechanism of its degradation of the non-phenolic arylglycerol beta-aryl ether substructure of lignin.</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="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></author><author><name sortKey="Kersten, P J" sort="Kersten, P J" uniqKey="Kersten P" first="P J" last="Kersten">P J Kersten</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="Kalyanaraman, B" sort="Kalyanaraman, B" uniqKey="Kalyanaraman B" first="B" last="Kalyanaraman">B. Kalyanaraman</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1986">1986</date><idno type="RBID">pubmed:3024619</idno><idno type="pmid">3024619</idno><idno type="pmc">PMC1146817</idno><idno type="doi">10.1042/bj2360279</idno><idno type="wicri:Area/Main/Corpus">001039</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001039</idno><idno type="wicri:Area/Main/Curation">001039</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001039</idno><idno type="wicri:Area/Main/Exploration">001039</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Ligninase of Phanerochaete chrysosporium. Mechanism of its degradation of the non-phenolic arylglycerol beta-aryl ether substructure of lignin.</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="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></author><author><name sortKey="Kersten, P J" sort="Kersten, P J" uniqKey="Kersten P" first="P J" last="Kersten">P J Kersten</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="Kalyanaraman, B" sort="Kalyanaraman, B" uniqKey="Kalyanaraman B" first="B" last="Kalyanaraman">B. Kalyanaraman</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="ISSN">0264-6021</idno><imprint><date when="1986" type="published">1986</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Fungi (enzymology)</term><term>Lignin (analogs & derivatives)</term><term>Lignin (metabolism)</term><term>Models, Chemical (MeSH)</term><term>Oxygenases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Champignons (enzymologie)</term><term>Lignine (analogues et dérivés)</term><term>Lignine (métabolisme)</term><term>Modèles chimiques (MeSH)</term><term>Oxygénases (métabolisme)</term><term>Sites de fixation (MeSH)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Champignons</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term><term>Oxygenases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term><term>Oxygénases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Electron Spin Resonance Spectroscopy</term><term>Models, Chemical</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Modèles chimiques</term><term>Sites de fixation</term><term>Spectroscopie de résonance de spin électronique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">This study examined the ligninase-catalysed degradation of lignin model compounds representing the arylglycerol beta-aryl ether substructure, which is the dominant one in the lignin polymer. Three dimeric model compounds were used, all methoxylated in the 3- and 4-positions of the arylglycerol ring (ring A) and having various substituents in the beta-ether-linked aromatic ring (ring B), so that competing reactions involving both rings could be compared. Studies of the products formed and the time courses of their formation showed that these model compounds are oxidized by ligninase (+ H2O2 + O2) in both ring A and ring B. The major consequence with all three model compounds is oxidation of ring A, leading primarily to cleavage between C(alpha) and C(beta) (C(alpha) being proximal to ring A), and to a lesser extent to the oxidation of the C(alpha)-hydroxy group to a carbonyl group. Such C(alpha)-oxidation deactivates ring A, leaving only ring B for attack. Studies with C(alpha)-carbonyl model compounds corresponding to the three basic model compounds revealed that oxidation of ring B leads in part to dealkoxylations (i.e. to cleavage of the glycerol beta-aryl ether bond and to demethoxylations), but that these are minor reactions in the model compounds most closely related to lignin. Evidence is also given that another consequence of oxidation of ring B in the C(alpha)-carbonyl model compounds is formation of unstable cyclohexadienone ketals, which can decompose with elimination of the beta-ether-linked aromatic ring. The mechanisms proposed for the observed reactions involve initial formation of aryl cation radicals in either ring A or ring B. The cation radical intermediate from one of the C(alpha)-carbonyl model compounds was identified by e.s.r. spectroscopy. The mechanisms are based on earlier studies showing that ligninase acts by oxidizing appropriately substituted aromatic nuclei to aryl cation radicals [Kersten, Tien, Kalyanaraman & Kirk (1985) J. Biol. Chem. 260, 2609-2612; Hammel, Tien, Kalyanaraman & Kirk (1985) J. Biol. Chem. 260, 8348-8353].</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">3024619</PMID><DateCompleted><Year>1987</Year><Month>01</Month><Day>22</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>236</Volume><Issue>1</Issue><PubDate><Year>1986</Year><Month>May</Month><Day>15</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Ligninase of Phanerochaete chrysosporium. Mechanism of its degradation of the non-phenolic arylglycerol beta-aryl ether substructure of lignin.</ArticleTitle><Pagination><MedlinePgn>279-87</MedlinePgn></Pagination><Abstract><AbstractText>This study examined the ligninase-catalysed degradation of lignin model compounds representing the arylglycerol beta-aryl ether substructure, which is the dominant one in the lignin polymer. Three dimeric model compounds were used, all methoxylated in the 3- and 4-positions of the arylglycerol ring (ring A) and having various substituents in the beta-ether-linked aromatic ring (ring B), so that competing reactions involving both rings could be compared. Studies of the products formed and the time courses of their formation showed that these model compounds are oxidized by ligninase (+ H2O2 + O2) in both ring A and ring B. The major consequence with all three model compounds is oxidation of ring A, leading primarily to cleavage between C(alpha) and C(beta) (C(alpha) being proximal to ring A), and to a lesser extent to the oxidation of the C(alpha)-hydroxy group to a carbonyl group. Such C(alpha)-oxidation deactivates ring A, leaving only ring B for attack. Studies with C(alpha)-carbonyl model compounds corresponding to the three basic model compounds revealed that oxidation of ring B leads in part to dealkoxylations (i.e. to cleavage of the glycerol beta-aryl ether bond and to demethoxylations), but that these are minor reactions in the model compounds most closely related to lignin. Evidence is also given that another consequence of oxidation of ring B in the C(alpha)-carbonyl model compounds is formation of unstable cyclohexadienone ketals, which can decompose with elimination of the beta-ether-linked aromatic ring. The mechanisms proposed for the observed reactions involve initial formation of aryl cation radicals in either ring A or ring B. The cation radical intermediate from one of the C(alpha)-carbonyl model compounds was identified by e.s.r. spectroscopy. The mechanisms are based on earlier studies showing that ligninase acts by oxidizing appropriately substituted aromatic nuclei to aryl cation radicals [Kersten, Tien, Kalyanaraman & Kirk (1985) J. Biol. Chem. 260, 2609-2612; Hammel, Tien, Kalyanaraman & Kirk (1985) J. Biol. Chem. 260, 8348-8353].</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kirk</LastName><ForeName>T K</ForeName><Initials>TK</Initials></Author><Author ValidYN="Y"><LastName>Tien</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kersten</LastName><ForeName>P J</ForeName><Initials>PJ</Initials></Author><Author ValidYN="Y"><LastName>Mozuch</LastName><ForeName>M D</ForeName><Initials>MD</Initials></Author><Author ValidYN="Y"><LastName>Kalyanaraman</LastName><ForeName>B</ForeName><Initials>B</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM-29035</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>RR-00108</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</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="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010105" MajorTopicYN="N">Oxygenases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1986</Year><Month>5</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1986</Year><Month>5</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1986</Year><Month>5</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">3024619</ArticleId><ArticleId IdType="pmc">PMC1146817</ArticleId><ArticleId IdType="doi">10.1042/bj2360279</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>J Bacteriol. 1981 Aug;147(2):471-6</Citation><ArticleIdList><ArticleId IdType="pubmed">7263612</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>Science. 1983 Aug 12;221(4611):661-3</Citation><ArticleIdList><ArticleId IdType="pubmed">17787736</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1984 Nov 1;234(2):353-62</Citation><ArticleIdList><ArticleId IdType="pubmed">6497376</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1985 Jul 15;260(14):8348-53</Citation><ArticleIdList><ArticleId IdType="pubmed">2989288</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1985 Mar 10;260(5):2609-12</Citation><ArticleIdList><ArticleId IdType="pubmed">2982828</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Kalyanaraman, B" sort="Kalyanaraman, B" uniqKey="Kalyanaraman B" first="B" last="Kalyanaraman">B. Kalyanaraman</name><name sortKey="Kersten, P J" sort="Kersten, P J" uniqKey="Kersten P" first="P J" last="Kersten">P J Kersten</name><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)
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