DetoxFungiV1, Main, Exploration, bibRecord, 002768

Interaction of 2,4,6-trinitrotoluene (TNT) and 4-amino-2,6-dinitrotoluene with humic monomers in the presence of oxidative enzymes.

Identifieur interne : 002768 ( Main/Exploration ); précédent : 002767; suivant : 002769

Interaction of 2,4,6-trinitrotoluene (TNT) and 4-amino-2,6-dinitrotoluene with humic monomers in the presence of oxidative enzymes.

Auteurs : C-J Wang [États-Unis] ; S. Thiele ; J-M Bollag

Source :

Archives of environmental contamination and toxicology [ 0090-4341 ] ; 2002.

RBID : pubmed:11706361

Descripteurs français

English descriptors

KwdEn :
- Aniline Compounds (chemistry), Aniline Compounds (metabolism), Horseradish Peroxidase (metabolism), Humic Substances (chemistry), Humic Substances (metabolism), Hydrogen-Ion Concentration (MeSH), Laccase (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (metabolism), Polymers (MeSH), Soil Microbiology (MeSH), Trinitrotoluene (chemistry), Trinitrotoluene (metabolism).
MESH :
- chemical , chemistry : Aniline Compounds, Humic Substances, Trinitrotoluene.
- chemical , metabolism : Aniline Compounds, Horseradish Peroxidase, Humic Substances, Oxidoreductases, Trinitrotoluene.
- Hydrogen-Ion Concentration, Laccase, Oxidation-Reduction, Polymers, Soil Microbiology.

Abstract

Oxidative coupling of nitroaromatic compounds involving soil organic matter was examined as a means of soil remediation. Humic monomers, serving as model compounds for soil humic substances, were used as cosubstrates, applying phenoloxidases (laccase from Trametes villosa and peroxidase from horseradish) as oxidative biocatalysts. Without the addition of a cosubstrate, only 30% of 4-amino-2,6-dinitrotoluene (4ADNT) and no 2,4,6-trinitrotoluene (TNT) were transformed in the presence of the laccase. Adding various phenolic monomers produced differing effects on the enzyme-mediated transformation, which indicated that xenobiotics are preferentially bound to quinoid and phenolic moieties of soil humic substances. In the presence of the humic monomer catechol and the enzyme, up to 100% of 4ADNT and up to 80% of TNT were transformed. Enzymatic transformation of 4ADNT in the presence of catechol reached a maximum at pH 6.8. TNT transformation, however, further increased at pH values above 6.8, even in the absence of the enzyme, due to chemical polymerization of catechol. We postulate a two-step reaction mechanism. The humic monomer is initially oxidized to a semi-quinone radical by a phenoloxidase. Subsequent oxidative coupling involves reactions with additional humic monomers or anilinic products derived from TNT, forming an anilinoquinone via nucleophilic addition or a benzoquinone-imine through condensation.

DOI: 10.1007/s002440010284
PubMed: 11706361

Affiliations:

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Le document en format XML

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<author><name sortKey="Wang, C J" sort="Wang, C J" uniqKey="Wang C" first="C-J" last="Wang">C-J Wang</name>
<affiliation wicri:level="4"><nlm:affiliation>Laboratory of Soil Biochemistry, Center for Bioremediation and Detoxification, 129 Land and Water Building, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.</nlm:affiliation>
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<placeName><settlement type="city">University Park (Pennsylvanie)</settlement>
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<author><name sortKey="Thiele, S" sort="Thiele, S" uniqKey="Thiele S" first="S" last="Thiele">S. Thiele</name>
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<author><name sortKey="Bollag, J M" sort="Bollag, J M" uniqKey="Bollag J" first="J-M" last="Bollag">J-M Bollag</name>
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<author><name sortKey="Wang, C J" sort="Wang, C J" uniqKey="Wang C" first="C-J" last="Wang">C-J Wang</name>
<affiliation wicri:level="4"><nlm:affiliation>Laboratory of Soil Biochemistry, Center for Bioremediation and Detoxification, 129 Land and Water Building, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.</nlm:affiliation>
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<author><name sortKey="Thiele, S" sort="Thiele, S" uniqKey="Thiele S" first="S" last="Thiele">S. Thiele</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aniline Compounds (chemistry)</term>
<term>Aniline Compounds (metabolism)</term>
<term>Horseradish Peroxidase (metabolism)</term>
<term>Humic Substances (chemistry)</term>
<term>Humic Substances (metabolism)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Laccase (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Polymers (MeSH)</term>
<term>Soil Microbiology (MeSH)</term>
<term>Trinitrotoluene (chemistry)</term>
<term>Trinitrotoluene (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>2,4,6-Trinitro-toluène (composition chimique)</term>
<term>2,4,6-Trinitro-toluène (métabolisme)</term>
<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Dérivés de l'aniline (composition chimique)</term>
<term>Dérivés de l'aniline (métabolisme)</term>
<term>Horseradish peroxidase (métabolisme)</term>
<term>Laccase (MeSH)</term>
<term>Microbiologie du sol (MeSH)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Polymères (MeSH)</term>
<term>Substances humiques (composition chimique)</term>
<term>Substances humiques (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Aniline Compounds</term>
<term>Humic Substances</term>
<term>Trinitrotoluene</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aniline Compounds</term>
<term>Horseradish Peroxidase</term>
<term>Humic Substances</term>
<term>Oxidoreductases</term>
<term>Trinitrotoluene</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>2,4,6-Trinitro-toluène</term>
<term>Dérivés de l'aniline</term>
<term>Substances humiques</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>2,4,6-Trinitro-toluène</term>
<term>Dérivés de l'aniline</term>
<term>Horseradish peroxidase</term>
<term>Oxidoreductases</term>
<term>Substances humiques</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term>
<term>Laccase</term>
<term>Oxidation-Reduction</term>
<term>Polymers</term>
<term>Soil Microbiology</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term>
<term>Laccase</term>
<term>Microbiologie du sol</term>
<term>Oxydoréduction</term>
<term>Polymères</term>
</keywords>
</textClass>
</profileDesc>
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<front><div type="abstract" xml:lang="en">Oxidative coupling of nitroaromatic compounds involving soil organic matter was examined as a means of soil remediation. Humic monomers, serving as model compounds for soil humic substances, were used as cosubstrates, applying phenoloxidases (laccase from Trametes villosa and peroxidase from horseradish) as oxidative biocatalysts. Without the addition of a cosubstrate, only 30% of 4-amino-2,6-dinitrotoluene (4ADNT) and no 2,4,6-trinitrotoluene (TNT) were transformed in the presence of the laccase. Adding various phenolic monomers produced differing effects on the enzyme-mediated transformation, which indicated that xenobiotics are preferentially bound to quinoid and phenolic moieties of soil humic substances. In the presence of the humic monomer catechol and the enzyme, up to 100% of 4ADNT and up to 80% of TNT were transformed. Enzymatic transformation of 4ADNT in the presence of catechol reached a maximum at pH 6.8. TNT transformation, however, further increased at pH values above 6.8, even in the absence of the enzyme, due to chemical polymerization of catechol. We postulate a two-step reaction mechanism. The humic monomer is initially oxidized to a semi-quinone radical by a phenoloxidase. Subsequent oxidative coupling involves reactions with additional humic monomers or anilinic products derived from TNT, forming an anilinoquinone via nucleophilic addition or a benzoquinone-imine through condensation.</div>
</front>
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<DateCompleted><Year>2002</Year>
<Month>02</Month>
<Day>26</Day>
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<DateRevised><Year>2006</Year>
<Month>11</Month>
<Day>15</Day>
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<Title>Archives of environmental contamination and toxicology</Title>
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<ArticleTitle>Interaction of 2,4,6-trinitrotoluene (TNT) and 4-amino-2,6-dinitrotoluene with humic monomers in the presence of oxidative enzymes.</ArticleTitle>
<Pagination><MedlinePgn>1-8</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Oxidative coupling of nitroaromatic compounds involving soil organic matter was examined as a means of soil remediation. Humic monomers, serving as model compounds for soil humic substances, were used as cosubstrates, applying phenoloxidases (laccase from Trametes villosa and peroxidase from horseradish) as oxidative biocatalysts. Without the addition of a cosubstrate, only 30% of 4-amino-2,6-dinitrotoluene (4ADNT) and no 2,4,6-trinitrotoluene (TNT) were transformed in the presence of the laccase. Adding various phenolic monomers produced differing effects on the enzyme-mediated transformation, which indicated that xenobiotics are preferentially bound to quinoid and phenolic moieties of soil humic substances. In the presence of the humic monomer catechol and the enzyme, up to 100% of 4ADNT and up to 80% of TNT were transformed. Enzymatic transformation of 4ADNT in the presence of catechol reached a maximum at pH 6.8. TNT transformation, however, further increased at pH values above 6.8, even in the absence of the enzyme, due to chemical polymerization of catechol. We postulate a two-step reaction mechanism. The humic monomer is initially oxidized to a semi-quinone radical by a phenoloxidase. Subsequent oxidative coupling involves reactions with additional humic monomers or anilinic products derived from TNT, forming an anilinoquinone via nucleophilic addition or a benzoquinone-imine through condensation.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>C-J</ForeName>
<Initials>CJ</Initials>
<AffiliationInfo><Affiliation>Laboratory of Soil Biochemistry, Center for Bioremediation and Detoxification, 129 Land and Water Building, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Thiele</LastName>
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<Chemical><RegistryNumber>118-96-7</RegistryNumber>
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<Chemical><RegistryNumber>19406-51-0</RegistryNumber>
<NameOfSubstance UI="C035207">4-amino-2,6-dinitrotoluene</NameOfSubstance>
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<Chemical><RegistryNumber>EC 1.-</RegistryNumber>
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<Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber>
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<Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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</MeshHeading>
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<Day>27</Day>
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<tree><noCountry><name sortKey="Bollag, J M" sort="Bollag, J M" uniqKey="Bollag J" first="J-M" last="Bollag">J-M Bollag</name>
<name sortKey="Thiele, S" sort="Thiele, S" uniqKey="Thiele S" first="S" last="Thiele">S. Thiele</name>
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<country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Wang, C J" sort="Wang, C J" uniqKey="Wang C" first="C-J" last="Wang">C-J Wang</name>
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Interaction of 2,4,6-trinitrotoluene (TNT) and 4-amino-2,6-dinitrotoluene with humic monomers in the presence of oxidative enzymes.

Interaction of 2,4,6-trinitrotoluene (TNT) and 4-amino-2,6-dinitrotoluene with humic monomers in the presence of oxidative enzymes.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki