Inactivating effect of phenolic unit structures on the biodegradation of lignin by lignin peroxidase from Phanerochaete chrysosporium.
Identifieur interne : 000287 ( Main/Exploration ); précédent : 000286; suivant : 000288Inactivating effect of phenolic unit structures on the biodegradation of lignin by lignin peroxidase from Phanerochaete chrysosporium.
Auteurs : Le Thanh Mai Pham [Corée du Sud] ; Moon-Ho Eom [Corée du Sud] ; Yong Hwan Kim [Corée du Sud]Source :
- Enzyme and microbial technology [ 1879-0909 ]
Descripteurs français
- KwdFr :
- Cinétique (MeSH), Domaine catalytique (MeSH), Dépollution biologique de l'environnement (MeSH), Hème (composition chimique), Lignine (analogues et dérivés), Lignine (composition chimique), Lignine (métabolisme), Peroxidases (composition chimique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Phénols (composition chimique), Protéines fongiques (composition chimique), Protéines fongiques (métabolisme), Structure moléculaire (MeSH), Transport d'électrons (MeSH), Tryptophane (composition chimique).
- MESH :
- analogues et dérivés : Lignine.
- composition chimique : Hème, Lignine, Peroxidases, Phénols, Protéines fongiques, Tryptophane.
- enzymologie : Phanerochaete.
- métabolisme : Lignine, Peroxidases, Protéines fongiques.
- Cinétique, Domaine catalytique, Dépollution biologique de l'environnement, Structure moléculaire, Transport d'électrons.
English descriptors
- KwdEn :
- Biodegradation, Environmental (MeSH), Catalytic Domain (MeSH), Electron Transport (MeSH), Fungal Proteins (chemistry), Fungal Proteins (metabolism), Heme (chemistry), Kinetics (MeSH), Lignin (analogs & derivatives), Lignin (chemistry), Lignin (metabolism), Molecular Structure (MeSH), Peroxidases (chemistry), Peroxidases (metabolism), Phanerochaete (enzymology), Phenols (chemistry), Tryptophan (chemistry).
- MESH :
- chemical , analogs & derivatives : Lignin.
- chemical , chemistry : Fungal Proteins, Heme, Lignin, Peroxidases, Phenols, Tryptophan.
- chemical , metabolism : Fungal Proteins, Lignin, Peroxidases.
- enzymology : Phanerochaete.
- Biodegradation, Environmental, Catalytic Domain, Electron Transport, Kinetics, Molecular Structure.
Abstract
An imbalance of electron in an intramolecular electron transfer pathway was identified as the central factor causing inefficient degradation of lignin by the lignin peroxidase H8 from Phanerochaete chrysosporium (LiPH8). It was elucidated that dimeric lignins or monolignolic analogs containing free-hydroxyl phenolic groups were not only favorable substrates for the reduction of LiPH8 but also strong inhibitors depressing the enzymatic degradation of lignin. The data collectively demonstrated that disturbing the interaction between the free OH group on the phenolic structure and the surface active sites around Trp171 caused the primary deficiency in electron transport between Trp171 and the heme site, which severely inhibited the efficiency of lignin biodegradation by LiPH8/H2O2.
DOI: 10.1016/j.enzmictec.2014.04.013
PubMed: 24910336
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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It was elucidated that dimeric lignins or monolignolic analogs containing free-hydroxyl phenolic groups were not only favorable substrates for the reduction of LiPH8 but also strong inhibitors depressing the enzymatic degradation of lignin. The data collectively demonstrated that disturbing the interaction between the free OH group on the phenolic structure and the surface active sites around Trp171 caused the primary deficiency in electron transport between Trp171 and the heme site, which severely inhibited the efficiency of lignin biodegradation by LiPH8/H2O2. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24910336</PMID><DateCompleted><Year>2015</Year><Month>05</Month><Day>11</Day></DateCompleted><DateRevised><Year>2014</Year><Month>06</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0909</ISSN><JournalIssue CitedMedium="Internet"><Volume>61-62</Volume><PubDate><MedlineDate>2014 Jul-Aug</MedlineDate></PubDate></JournalIssue><Title>Enzyme and microbial technology</Title><ISOAbbreviation>Enzyme Microb Technol</ISOAbbreviation></Journal><ArticleTitle>Inactivating effect of phenolic unit structures on the biodegradation of lignin by lignin peroxidase from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>48-54</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.enzmictec.2014.04.013</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0141-0229(14)00086-6</ELocationID><Abstract><AbstractText>An imbalance of electron in an intramolecular electron transfer pathway was identified as the central factor causing inefficient degradation of lignin by the lignin peroxidase H8 from Phanerochaete chrysosporium (LiPH8). It was elucidated that dimeric lignins or monolignolic analogs containing free-hydroxyl phenolic groups were not only favorable substrates for the reduction of LiPH8 but also strong inhibitors depressing the enzymatic degradation of lignin. The data collectively demonstrated that disturbing the interaction between the free OH group on the phenolic structure and the surface active sites around Trp171 caused the primary deficiency in electron transport between Trp171 and the heme site, which severely inhibited the efficiency of lignin biodegradation by LiPH8/H2O2. </AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Thanh Mai Pham</LastName><ForeName>Le</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-Dong, Nowon-Gu, Seoul 139-701, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Eom</LastName><ForeName>Moon-Ho</ForeName><Initials>MH</Initials><AffiliationInfo><Affiliation>Biofuel and Biochemical Team, R&D Center, GS Caltex Corporation, 104-4, Munji-dong, Yusung-gu, Daejeon-city 305-380, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Yong Hwan</ForeName><Initials>YH</Initials><AffiliationInfo><Affiliation>Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-Dong, Nowon-Gu, Seoul 139-701, Republic of Korea. Electronic address: metalkim@kw.ac.kr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>05</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Enzyme Microb Technol</MedlineTA><NlmUniqueID>8003761</NlmUniqueID><ISSNLinking>0141-0229</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010636">Phenols</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><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="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Electron transfer pathway</Keyword><Keyword MajorTopicYN="N">Free-hydroxyl phenolic compound</Keyword><Keyword MajorTopicYN="N">Lignin peroxidase isozyme H8</Keyword><Keyword MajorTopicYN="N">Phanerochaete chrysosporium</Keyword><Keyword MajorTopicYN="N">Surface active site</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>03</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>04</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>04</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>6</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>6</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>5</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24910336</ArticleId><ArticleId IdType="pii">S0141-0229(14)00086-6</ArticleId><ArticleId 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