Thiol-mediated oxidation of nonphenolic lignin model compounds by manganese peroxidase of Phanerochaete chrysosporium.
Identifieur interne : 000F79 ( Main/Exploration ); précédent : 000F78; suivant : 000F80Thiol-mediated oxidation of nonphenolic lignin model compounds by manganese peroxidase of Phanerochaete chrysosporium.
Auteurs : H. Wariishi ; K. Valli ; V. Renganathan ; M H GoldSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1989.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Basidiomycota.
- métabolisme : Lignine.
- Alcools benzyliques, Anaérobiose, Aérobiose, Modèles chimiques, Oxydoréduction, Peroxidases, Spécificité du substrat, Thiols.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Lignin.
- chemical : Benzyl Alcohols, Peroxidases, Sulfhydryl Compounds.
- enzymology : Basidiomycota.
- Aerobiosis, Anaerobiosis, Models, Chemical, Oxidation-Reduction, Substrate Specificity.
Abstract
In the presence of MnII, H2O2, and glutathione (GSH), manganese peroxidase oxidized veratryl alcohol (I) to veratraldehyde (IV). Anisyl alcohol (II) and benzyl alcohol (III) were also oxidized by this system to their corresponding aldehydes (V and VI). In the presence of GSH, chemically prepared MnIII or gamma-irradiation also catalyzed the oxidation of I, II, and III to IV, V, and VI, respectively. GSH and dithiothreitol rapidly reduced MnIII to MnII in the absence of aromatic substrates and the dithiothreitol was oxidized to its disulfide (4,5-dihydroxyl-1,2-dithiane). These results indicate that the thiol is oxidized by enzyme-generated MnIII to a thiyl radical. The latter abstracts a hydrogen from the substrate, forming a benzylic radical which reacts with another thiyl radical to yield an intermediate which decomposes to the benzaldehyde product. In the presence of MnII, GSH, and H2O2, manganese peroxidase also oxidized 1-(4-ethoxy-3-methoxy-phenyl)-2-(4'-hydroxymethyl-2'-methoxyphenoxy)- 1,3-dihydroxypropane (XII) to yield vanillyl alcohol (VII), vanillin (VIII), 1-(4-ethoxy-3-methoxyphenyl)-1,3-dihydroxypropane (XVI), 1-(4-ethoxy-3-methoxyphenyl)-1-oxo-3-hydroxypropane (XIX), and several C alpha oxidized dimeric products. Abstraction of the C alpha (A ring) hydrogen of the dimer (XII) yields a benzylic radical, leading to C beta oxygen ether cleavage. The resultant intermediates yield the ketone (XIX) and vanillyl alcohol (VII) or vanillin (VIII). Alternatively, benzylic radical formation at the C' alpha position (B ring) leads to radical cleavage, yielding a quinone methide and a C beta radical, which yield vanillin and the 1,3-diol (XVI), respectively. In these reactions, MnIII oxidizes a thiol to a thiyl radical which subsequently abstracts a hydrogen from the substrate to form a benzylic radical. The latter undergoes nonenzymatic reactions to yield the final products.
PubMed: 2760063
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Thiol-mediated oxidation of nonphenolic lignin model compounds by manganese peroxidase of Phanerochaete chrysosporium.</title><author><name sortKey="Wariishi, H" sort="Wariishi, H" uniqKey="Wariishi H" first="H" last="Wariishi">H. Wariishi</name><affiliation><nlm:affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Center, Beaverton 97006-1999.</nlm:affiliation><wicri:noCountry code="subField">Beaverton 97006-1999</wicri:noCountry></affiliation></author><author><name sortKey="Valli, K" sort="Valli, K" uniqKey="Valli K" first="K" last="Valli">K. Valli</name></author><author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></author><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1989">1989</date><idno type="RBID">pubmed:2760063</idno><idno type="pmid">2760063</idno><idno type="wicri:Area/Main/Corpus">000F83</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000F83</idno><idno type="wicri:Area/Main/Curation">000F83</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000F83</idno><idno type="wicri:Area/Main/Exploration">000F83</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Thiol-mediated oxidation of nonphenolic lignin model compounds by manganese peroxidase of Phanerochaete chrysosporium.</title><author><name sortKey="Wariishi, H" sort="Wariishi, H" uniqKey="Wariishi H" first="H" last="Wariishi">H. Wariishi</name><affiliation><nlm:affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Center, Beaverton 97006-1999.</nlm:affiliation><wicri:noCountry code="subField">Beaverton 97006-1999</wicri:noCountry></affiliation></author><author><name sortKey="Valli, K" sort="Valli, K" uniqKey="Valli K" first="K" last="Valli">K. Valli</name></author><author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></author><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1989" type="published">1989</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aerobiosis (MeSH)</term><term>Anaerobiosis (MeSH)</term><term>Basidiomycota (enzymology)</term><term>Benzyl Alcohols (MeSH)</term><term>Lignin (metabolism)</term><term>Models, Chemical (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Sulfhydryl Compounds (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcools benzyliques (MeSH)</term><term>Anaérobiose (MeSH)</term><term>Aérobiose (MeSH)</term><term>Basidiomycota (enzymologie)</term><term>Lignine (métabolisme)</term><term>Modèles chimiques (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Thiols (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Benzyl Alcohols</term><term>Peroxidases</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Aerobiosis</term><term>Anaerobiosis</term><term>Models, Chemical</term><term>Oxidation-Reduction</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alcools benzyliques</term><term>Anaérobiose</term><term>Aérobiose</term><term>Modèles chimiques</term><term>Oxydoréduction</term><term>Peroxidases</term><term>Spécificité du substrat</term><term>Thiols</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In the presence of MnII, H2O2, and glutathione (GSH), manganese peroxidase oxidized veratryl alcohol (I) to veratraldehyde (IV). Anisyl alcohol (II) and benzyl alcohol (III) were also oxidized by this system to their corresponding aldehydes (V and VI). In the presence of GSH, chemically prepared MnIII or gamma-irradiation also catalyzed the oxidation of I, II, and III to IV, V, and VI, respectively. GSH and dithiothreitol rapidly reduced MnIII to MnII in the absence of aromatic substrates and the dithiothreitol was oxidized to its disulfide (4,5-dihydroxyl-1,2-dithiane). These results indicate that the thiol is oxidized by enzyme-generated MnIII to a thiyl radical. The latter abstracts a hydrogen from the substrate, forming a benzylic radical which reacts with another thiyl radical to yield an intermediate which decomposes to the benzaldehyde product. In the presence of MnII, GSH, and H2O2, manganese peroxidase also oxidized 1-(4-ethoxy-3-methoxy-phenyl)-2-(4'-hydroxymethyl-2'-methoxyphenoxy)- 1,3-dihydroxypropane (XII) to yield vanillyl alcohol (VII), vanillin (VIII), 1-(4-ethoxy-3-methoxyphenyl)-1,3-dihydroxypropane (XVI), 1-(4-ethoxy-3-methoxyphenyl)-1-oxo-3-hydroxypropane (XIX), and several C alpha oxidized dimeric products. Abstraction of the C alpha (A ring) hydrogen of the dimer (XII) yields a benzylic radical, leading to C beta oxygen ether cleavage. The resultant intermediates yield the ketone (XIX) and vanillyl alcohol (VII) or vanillin (VIII). Alternatively, benzylic radical formation at the C' alpha position (B ring) leads to radical cleavage, yielding a quinone methide and a C beta radical, which yield vanillin and the 1,3-diol (XVI), respectively. In these reactions, MnIII oxidizes a thiol to a thiyl radical which subsequently abstracts a hydrogen from the substrate to form a benzylic radical. The latter undergoes nonenzymatic reactions to yield the final products.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2760063</PMID><DateCompleted><Year>1989</Year><Month>09</Month><Day>13</Day></DateCompleted><DateRevised><Year>2012</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>264</Volume><Issue>24</Issue><PubDate><Year>1989</Year><Month>Aug</Month><Day>25</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Thiol-mediated oxidation of nonphenolic lignin model compounds by manganese peroxidase of Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>14185-91</MedlinePgn></Pagination><Abstract><AbstractText>In the presence of MnII, H2O2, and glutathione (GSH), manganese peroxidase oxidized veratryl alcohol (I) to veratraldehyde (IV). Anisyl alcohol (II) and benzyl alcohol (III) were also oxidized by this system to their corresponding aldehydes (V and VI). In the presence of GSH, chemically prepared MnIII or gamma-irradiation also catalyzed the oxidation of I, II, and III to IV, V, and VI, respectively. GSH and dithiothreitol rapidly reduced MnIII to MnII in the absence of aromatic substrates and the dithiothreitol was oxidized to its disulfide (4,5-dihydroxyl-1,2-dithiane). These results indicate that the thiol is oxidized by enzyme-generated MnIII to a thiyl radical. The latter abstracts a hydrogen from the substrate, forming a benzylic radical which reacts with another thiyl radical to yield an intermediate which decomposes to the benzaldehyde product. In the presence of MnII, GSH, and H2O2, manganese peroxidase also oxidized 1-(4-ethoxy-3-methoxy-phenyl)-2-(4'-hydroxymethyl-2'-methoxyphenoxy)- 1,3-dihydroxypropane (XII) to yield vanillyl alcohol (VII), vanillin (VIII), 1-(4-ethoxy-3-methoxyphenyl)-1,3-dihydroxypropane (XVI), 1-(4-ethoxy-3-methoxyphenyl)-1-oxo-3-hydroxypropane (XIX), and several C alpha oxidized dimeric products. Abstraction of the C alpha (A ring) hydrogen of the dimer (XII) yields a benzylic radical, leading to C beta oxygen ether cleavage. The resultant intermediates yield the ketone (XIX) and vanillyl alcohol (VII) or vanillin (VIII). Alternatively, benzylic radical formation at the C' alpha position (B ring) leads to radical cleavage, yielding a quinone methide and a C beta radical, which yield vanillin and the 1,3-diol (XVI), respectively. In these reactions, MnIII oxidizes a thiol to a thiyl radical which subsequently abstracts a hydrogen from the substrate to form a benzylic radical. The latter undergoes nonenzymatic reactions to yield the final products.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wariishi</LastName><ForeName>H</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Center, Beaverton 97006-1999.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Valli</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Renganathan</LastName><ForeName>V</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Gold</LastName><ForeName>M H</ForeName><Initials>MH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</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 1.11.1.13</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="D000332" MajorTopicYN="N">Aerobiosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000693" MajorTopicYN="N">Anaerobiosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="Y">Peroxidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="Y">Sulfhydryl Compounds</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1989</Year><Month>8</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1989</Year><Month>8</Month><Day>25</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1989</Year><Month>8</Month><Day>25</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2760063</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name><name sortKey="Valli, K" sort="Valli, K" uniqKey="Valli K" first="K" last="Valli">K. Valli</name><name sortKey="Wariishi, H" sort="Wariishi, H" uniqKey="Wariishi H" first="H" last="Wariishi">H. Wariishi</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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