Lignin peroxidase-catalyzed oxidation of sulfonated azo dyes generates novel sulfophenyl hydroperoxides.
Identifieur interne : 000D03 ( Main/Exploration ); précédent : 000D02; suivant : 000D04Lignin peroxidase-catalyzed oxidation of sulfonated azo dyes generates novel sulfophenyl hydroperoxides.
Auteurs : M. Chivukula [États-Unis] ; J T Spadaro ; V. RenganathanSource :
- Biochemistry [ 0006-2960 ] ; 1995.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Basidiomycota.
- métabolisme : Benzènesulfonates, Composés azoïques, Naphtalènesulfonates, Peroxidases, Peroxydes.
- Agents colorants, Oxydoréduction, Spectrométrie de masse.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Azo Compounds, Benzenesulfonates, Naphthalenesulfonates, Peroxidases, Peroxides.
- enzymology : Basidiomycota.
- chemical : Coloring Agents, Mass Spectrometry, Oxidation-Reduction.
Abstract
Lignin peroxidase (LiP) is an extracellular enzyme produced by the lignin-degrading fungus Phanerochaete chrysosporium and is involved in azo dye degradation by this organism. In this study, LiP oxidation of the sulfonated azo dyes 4-(4'-sulfophenylazo)-2,6- dimethylphenol (I), Orange II [1-(4'-sulfophenylazo)-2-naphthol] (II), a dimethyl analog of Orange II [1-(2',6'-dimethyl-4'-sulfophenylazo)-2-naphthol] (III), and 4-(4'-sulfonamidophenylazo)-2,6-dimehtylphenol (IV) was examined. Azo dye I was oxidized to 2,6-dimethyl-1,4-benzoquinone and 4-sulfophenyl hydroperoxide. Orange II (II) was oxidized to 1,2-naphthoquinone and 4-sulfophenyl hydroperoxide. The dimethyl analog of Orange II (III) was oxidized to 1,2-naphthoquinone and 2,6-dimethyl-4-sulfophenyl hydroperoxide. Azo dye IV was oxidized predominantly to 2,6-dimethyl-1,4-benzoquinone and another product, tentatively characterized as 4-sulfonamidophenyl hydroperoxide. In the 18O-labeling studies with 18O2, oxygen incorporation into the phenyl hydroperoxides from the oxidation of I and III was observed. A mechanism for azo dye degradation consistent with product identification and the 18O-labeling studies is proposed. Two successive one-electron oxidations of the phenolic ring of an azo dye by the H2O2-oxidized forms of LiP produces a carbonium ion. Then water attacks the phenolic carbon bearing the azo linkage, producing an unstable hydroxy intermediate which breaks down to yield a quinone and a sulfo- or sulfonamidophenyldiazene. The phenyldiazene is oxidized by O2 to generate the corresponding phenyldiazene radical, which eliminates N2 to yield a sulfo- or sulfonamidophenyl radical. O2 scavenges the latter to yield the corresponding hydroperoxide.(ABSTRACT TRUNCATED AT 250 WORDS)
DOI: 10.1021/bi00023a024
PubMed: 7779823
Affiliations:
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Chivukula</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland 97291-1000, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland 97291-1000</wicri:regionArea><placeName><settlement type="city">Portland</settlement><region type="state">Oregon</region></placeName></affiliation></author><author><name sortKey="Spadaro, J T" sort="Spadaro, J T" uniqKey="Spadaro J" first="J T" last="Spadaro">J T Spadaro</name></author><author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1995">1995</date><idno type="RBID">pubmed:7779823</idno><idno type="pmid">7779823</idno><idno type="doi">10.1021/bi00023a024</idno><idno type="wicri:Area/Main/Corpus">000D04</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D04</idno><idno type="wicri:Area/Main/Curation">000D04</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D04</idno><idno type="wicri:Area/Main/Exploration">000D04</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Lignin peroxidase-catalyzed oxidation of sulfonated azo dyes generates novel sulfophenyl hydroperoxides.</title><author><name sortKey="Chivukula, M" sort="Chivukula, M" uniqKey="Chivukula M" first="M" last="Chivukula">M. Chivukula</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland 97291-1000, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland 97291-1000</wicri:regionArea><placeName><settlement type="city">Portland</settlement><region type="state">Oregon</region></placeName></affiliation></author><author><name sortKey="Spadaro, J T" sort="Spadaro, J T" uniqKey="Spadaro J" first="J T" last="Spadaro">J T Spadaro</name></author><author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="1995" type="published">1995</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Azo Compounds (metabolism)</term><term>Basidiomycota (enzymology)</term><term>Benzenesulfonates (metabolism)</term><term>Coloring Agents (MeSH)</term><term>Mass Spectrometry (MeSH)</term><term>Naphthalenesulfonates (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (metabolism)</term><term>Peroxides (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agents colorants (MeSH)</term><term>Basidiomycota (enzymologie)</term><term>Benzènesulfonates (métabolisme)</term><term>Composés azoïques (métabolisme)</term><term>Naphtalènesulfonates (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (métabolisme)</term><term>Peroxydes (métabolisme)</term><term>Spectrométrie de masse (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Azo Compounds</term><term>Benzenesulfonates</term><term>Naphthalenesulfonates</term><term>Peroxidases</term><term>Peroxides</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>Benzènesulfonates</term><term>Composés azoïques</term><term>Naphtalènesulfonates</term><term>Peroxidases</term><term>Peroxydes</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Coloring Agents</term><term>Mass Spectrometry</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Agents colorants</term><term>Oxydoréduction</term><term>Spectrométrie de masse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignin peroxidase (LiP) is an extracellular enzyme produced by the lignin-degrading fungus Phanerochaete chrysosporium and is involved in azo dye degradation by this organism. In this study, LiP oxidation of the sulfonated azo dyes 4-(4'-sulfophenylazo)-2,6- dimethylphenol (I), Orange II [1-(4'-sulfophenylazo)-2-naphthol] (II), a dimethyl analog of Orange II [1-(2',6'-dimethyl-4'-sulfophenylazo)-2-naphthol] (III), and 4-(4'-sulfonamidophenylazo)-2,6-dimehtylphenol (IV) was examined. Azo dye I was oxidized to 2,6-dimethyl-1,4-benzoquinone and 4-sulfophenyl hydroperoxide. Orange II (II) was oxidized to 1,2-naphthoquinone and 4-sulfophenyl hydroperoxide. The dimethyl analog of Orange II (III) was oxidized to 1,2-naphthoquinone and 2,6-dimethyl-4-sulfophenyl hydroperoxide. Azo dye IV was oxidized predominantly to 2,6-dimethyl-1,4-benzoquinone and another product, tentatively characterized as 4-sulfonamidophenyl hydroperoxide. In the 18O-labeling studies with 18O2, oxygen incorporation into the phenyl hydroperoxides from the oxidation of I and III was observed. A mechanism for azo dye degradation consistent with product identification and the 18O-labeling studies is proposed. Two successive one-electron oxidations of the phenolic ring of an azo dye by the H2O2-oxidized forms of LiP produces a carbonium ion. Then water attacks the phenolic carbon bearing the azo linkage, producing an unstable hydroxy intermediate which breaks down to yield a quinone and a sulfo- or sulfonamidophenyldiazene. The phenyldiazene is oxidized by O2 to generate the corresponding phenyldiazene radical, which eliminates N2 to yield a sulfo- or sulfonamidophenyl radical. O2 scavenges the latter to yield the corresponding hydroperoxide.(ABSTRACT TRUNCATED AT 250 WORDS)</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7779823</PMID><DateCompleted><Year>1995</Year><Month>07</Month><Day>19</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>34</Volume><Issue>23</Issue><PubDate><Year>1995</Year><Month>Jun</Month><Day>13</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Lignin peroxidase-catalyzed oxidation of sulfonated azo dyes generates novel sulfophenyl hydroperoxides.</ArticleTitle><Pagination><MedlinePgn>7765-72</MedlinePgn></Pagination><Abstract><AbstractText>Lignin peroxidase (LiP) is an extracellular enzyme produced by the lignin-degrading fungus Phanerochaete chrysosporium and is involved in azo dye degradation by this organism. In this study, LiP oxidation of the sulfonated azo dyes 4-(4'-sulfophenylazo)-2,6- dimethylphenol (I), Orange II [1-(4'-sulfophenylazo)-2-naphthol] (II), a dimethyl analog of Orange II [1-(2',6'-dimethyl-4'-sulfophenylazo)-2-naphthol] (III), and 4-(4'-sulfonamidophenylazo)-2,6-dimehtylphenol (IV) was examined. Azo dye I was oxidized to 2,6-dimethyl-1,4-benzoquinone and 4-sulfophenyl hydroperoxide. Orange II (II) was oxidized to 1,2-naphthoquinone and 4-sulfophenyl hydroperoxide. The dimethyl analog of Orange II (III) was oxidized to 1,2-naphthoquinone and 2,6-dimethyl-4-sulfophenyl hydroperoxide. Azo dye IV was oxidized predominantly to 2,6-dimethyl-1,4-benzoquinone and another product, tentatively characterized as 4-sulfonamidophenyl hydroperoxide. In the 18O-labeling studies with 18O2, oxygen incorporation into the phenyl hydroperoxides from the oxidation of I and III was observed. A mechanism for azo dye degradation consistent with product identification and the 18O-labeling studies is proposed. Two successive one-electron oxidations of the phenolic ring of an azo dye by the H2O2-oxidized forms of LiP produces a carbonium ion. Then water attacks the phenolic carbon bearing the azo linkage, producing an unstable hydroxy intermediate which breaks down to yield a quinone and a sulfo- or sulfonamidophenyldiazene. The phenyldiazene is oxidized by O2 to generate the corresponding phenyldiazene radical, which eliminates N2 to yield a sulfo- or sulfonamidophenyl radical. O2 scavenges the latter to yield the corresponding hydroperoxide.(ABSTRACT TRUNCATED AT 250 WORDS)</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chivukula</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland 97291-1000, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Spadaro</LastName><ForeName>J T</ForeName><Initials>JT</Initials></Author><Author ValidYN="Y"><LastName>Renganathan</LastName><ForeName>V</ForeName><Initials>V</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>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001391">Azo Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001557">Benzenesulfonates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004396">Coloring Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009282">Naphthalenesulfonates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010545">Peroxides</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="D001391" MajorTopicYN="N">Azo Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001557" MajorTopicYN="N">Benzenesulfonates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004396" MajorTopicYN="N">Coloring Agents</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009282" MajorTopicYN="N">Naphthalenesulfonates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010545" MajorTopicYN="N">Peroxides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1995</Year><Month>6</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1995</Year><Month>6</Month><Day>13</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1995</Year><Month>6</Month><Day>13</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7779823</ArticleId><ArticleId IdType="doi">10.1021/bi00023a024</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Oregon</li></region><settlement><li>Portland</li></settlement></list><tree><noCountry><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name><name sortKey="Spadaro, J T" sort="Spadaro, J T" uniqKey="Spadaro J" first="J T" last="Spadaro">J T Spadaro</name></noCountry><country name="États-Unis"><region name="Oregon"><name sortKey="Chivukula, M" sort="Chivukula, M" uniqKey="Chivukula M" first="M" last="Chivukula">M. Chivukula</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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