Lignin dehydrogenative polymerization mechanism: a poplar cell wall peroxidase directly oxidizes polymer lignin and produces in vitro dehydrogenative polymer rich in beta-O-4 linkage.
Identifieur interne : 004312 ( Main/Curation ); précédent : 004311; suivant : 004313Lignin dehydrogenative polymerization mechanism: a poplar cell wall peroxidase directly oxidizes polymer lignin and produces in vitro dehydrogenative polymer rich in beta-O-4 linkage.
Auteurs : Shinya Sasaki [Japon] ; Tomoaki Nishida ; Yuji Tsutsumi ; Ryuichiro KondoSource :
- FEBS letters [ 0014-5793 ] ; 2004.
Descripteurs français
- KwdFr :
- Alcools (métabolisme), Cytochromes c (métabolisme), Lignine (composition chimique), Lignine (métabolisme), Oxydoréduction (MeSH), Paroi cellulaire (composition chimique), Paroi cellulaire (enzymologie), Peroxidases (métabolisme), Phénols (métabolisme), Polymères (composition chimique), Populus (anatomie et histologie), Populus (composition chimique), Populus (métabolisme), Protéines végétales (métabolisme).
- MESH :
- anatomie et histologie : Populus.
- composition chimique : Lignine, Paroi cellulaire, Polymères, Populus.
- enzymologie : Paroi cellulaire.
- métabolisme : Alcools, Cytochromes c, Lignine, Peroxidases, Phénols, Populus, Protéines végétales.
- Oxydoréduction.
English descriptors
- KwdEn :
- Alcohols (metabolism), Cell Wall (chemistry), Cell Wall (enzymology), Cytochromes c (metabolism), Lignin (chemistry), Lignin (metabolism), Oxidation-Reduction (MeSH), Peroxidases (metabolism), Phenols (metabolism), Plant Proteins (metabolism), Polymers (chemistry), Populus (anatomy & histology), Populus (chemistry), Populus (metabolism).
- MESH :
- chemical , chemistry : Lignin, Polymers.
- chemical , metabolism : Alcohols, Cytochromes c, Lignin, Peroxidases, Phenols, Plant Proteins.
- anatomy & histology : Populus.
- chemistry : Cell Wall, Populus.
- enzymology : Cell Wall.
- metabolism : Populus.
- Oxidation-Reduction.
Abstract
An investigation was performed to determine whether lignin dehydrogenative polymerization proceeds via radical mediation or direct oxidation by peroxidases. It was found that coniferyl alcohol radical transferred quickly to sinapyl alcohol. The transfer to syringaresinol was slower, however, the transfer to polymeric lignols occurred very slightly. This result suggests that the radical mediator theory does not sufficiently explain the mechanism for dehydrogenative polymerization of lignin. A cationic cell wall peroxidase (CWPO-C) from poplar (Populus alba L.) callus showed a strong substrate preference for sinapyl alcohol and the sinapyl alcohol dimer, syringaresinol. Moreover, CWPO-C was capable of oxidizing high-molecular-weight sinapyl alcohol polymers and ferrocytochrome c. Therefore, the CWPO-C characteristics are important to produce polymer lignin. The results suggest that CWPO-C may be a peroxidase isoenzyme responsible for the lignification of plant cell walls.
DOI: 10.1016/S0014-5793(04)00224-8
PubMed: 15044025
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uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name></author><author><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15044025</idno><idno type="pmid">15044025</idno><idno type="doi">10.1016/S0014-5793(04)00224-8</idno><idno type="wicri:Area/Main/Corpus">004312</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004312</idno><idno type="wicri:Area/Main/Curation">004312</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004312</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Lignin dehydrogenative polymerization mechanism: a poplar cell wall peroxidase directly oxidizes polymer lignin and produces in vitro dehydrogenative polymer rich in beta-O-4 linkage.</title><author><name sortKey="Sasaki, Shinya" sort="Sasaki, Shinya" uniqKey="Sasaki S" first="Shinya" last="Sasaki">Shinya Sasaki</name><affiliation wicri:level="1"><nlm:affiliation>Department of Forest and Forest Products Sciences, Kyushu University, 6-10-1 Hakozaki, Higashiku, Fukuoka 812-8581, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Forest and Forest Products Sciences, Kyushu University, 6-10-1 Hakozaki, Higashiku, Fukuoka 812-8581</wicri:regionArea></affiliation></author><author><name sortKey="Nishida, Tomoaki" sort="Nishida, Tomoaki" uniqKey="Nishida T" first="Tomoaki" last="Nishida">Tomoaki Nishida</name></author><author><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name></author><author><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name></author></analytic><series><title 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(composition chimique)</term><term>Paroi cellulaire (enzymologie)</term><term>Peroxidases (métabolisme)</term><term>Phénols (métabolisme)</term><term>Polymères (composition chimique)</term><term>Populus (anatomie et histologie)</term><term>Populus (composition chimique)</term><term>Populus (métabolisme)</term><term>Protéines végétales (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lignin</term><term>Polymers</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohols</term><term>Cytochromes c</term><term>Lignin</term><term>Peroxidases</term><term>Phenols</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="anatomie et histologie" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="anatomy & histology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Wall</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Lignine</term><term>Paroi cellulaire</term><term>Polymères</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Paroi cellulaire</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cell Wall</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcools</term><term>Cytochromes c</term><term>Lignine</term><term>Peroxidases</term><term>Phénols</term><term>Populus</term><term>Protéines végétales</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">An investigation was performed to determine whether lignin dehydrogenative polymerization proceeds via radical mediation or direct oxidation by peroxidases. It was found that coniferyl alcohol radical transferred quickly to sinapyl alcohol. The transfer to syringaresinol was slower, however, the transfer to polymeric lignols occurred very slightly. This result suggests that the radical mediator theory does not sufficiently explain the mechanism for dehydrogenative polymerization of lignin. A cationic cell wall peroxidase (CWPO-C) from poplar (Populus alba L.) callus showed a strong substrate preference for sinapyl alcohol and the sinapyl alcohol dimer, syringaresinol. Moreover, CWPO-C was capable of oxidizing high-molecular-weight sinapyl alcohol polymers and ferrocytochrome c. Therefore, the CWPO-C characteristics are important to produce polymer lignin. The results suggest that CWPO-C may be a peroxidase isoenzyme responsible for the lignification of plant cell walls.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15044025</PMID><DateCompleted><Year>2004</Year><Month>05</Month><Day>11</Day></DateCompleted><DateRevised><Year>2012</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>562</Volume><Issue>1-3</Issue><PubDate><Year>2004</Year><Month>Mar</Month><Day>26</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Lignin dehydrogenative polymerization mechanism: a poplar cell wall peroxidase directly oxidizes polymer lignin and produces in vitro dehydrogenative polymer rich in beta-O-4 linkage.</ArticleTitle><Pagination><MedlinePgn>197-201</MedlinePgn></Pagination><Abstract><AbstractText>An investigation was performed to determine whether lignin dehydrogenative polymerization proceeds via radical mediation or direct oxidation by peroxidases. 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