Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes.
Identifieur interne : 000F61 ( Main/Exploration ); précédent : 000F60; suivant : 000F62Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes.
Auteurs : P J Kersten [États-Unis] ; B. Kalyanaraman ; K E Hammel ; B. Reinhammar ; T K KirkSource :
- The Biochemical journal [ 0264-6021 ] ; 1990.
Descripteurs français
- KwdFr :
- Chrysosporium (enzymologie), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Deuteromycota (enzymologie), Dérivés du benzène (métabolisme), Horseradish peroxidase (métabolisme), Laccase (MeSH), Oxidoreductases (métabolisme), Peroxidases (métabolisme), Spectrophotométrie UV (MeSH), Spectroscopie de résonance de spin électronique (MeSH).
- MESH :
English descriptors
- KwdEn :
- Benzene Derivatives (metabolism), Chrysosporium (enzymology), Electron Spin Resonance Spectroscopy (MeSH), Horseradish Peroxidase (metabolism), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), Laccase (MeSH), Mitosporic Fungi (enzymology), Oxidoreductases (metabolism), Peroxidases (metabolism), Spectrophotometry, Ultraviolet (MeSH).
- MESH :
- chemical , metabolism : Benzene Derivatives, Horseradish Peroxidase, Oxidoreductases, Peroxidases.
- enzymology : Chrysosporium, Mitosporic Fungi.
- Electron Spin Resonance Spectroscopy, Hydrogen-Ion Concentration, Kinetics, Laccase, Spectrophotometry, Ultraviolet.
Abstract
Lignin peroxidase oxidizes non-phenolic substrates by one electron to give aryl-cation-radical intermediates, which react further to give a variety of products. The present study investigated the possibility that other peroxidative and oxidative enzymes known to catalyse one-electron oxidations may also oxidize non-phenolics to cation-radical intermediates and that this ability is related to the redox potential of the substrate. Lignin peroxidase from the fungus Phanerochaete chrysosporium, horseradish peroxidase (HRP) and laccase from the fungus Trametes versicolor were chosen for investigation with methoxybenzenes as a homologous series of substrates. The twelve methoxybenzene congeners have known half-wave potentials that differ by as much as approximately 1 V. Lignin peroxidase oxidized the ten with the lowest half-wave potentials, whereas HRP oxidized the four lowest and laccase oxidized only 1,2,4,5-tetramethoxybenzene, the lowest. E.s.r. spectroscopy showed that this congener is oxidized to its cation radical by all three enzymes. Oxidation in each case gave the same products: 2,5-dimethoxy-p-benzoquinone and 4,5-dimethoxy-o-benzoquinone, in a 4:1 ratio, plus 2 mol of methanol for each 1 mol of substrate. Using HRP-catalysed oxidation, we showed that the quinone oxygen atoms are derived from water. We conclude that the three enzymes affect their substrates similarly, and that whether an aromatic compound is a substrate depends in large part on its redox potential. Furthermore, oxidized lignin peroxidase is clearly a stronger oxidant than oxidized HRP or laccase. Determination of the enzyme kinetic parameters for the methoxybenzene oxidations demonstrated further differences among the enzymes.
DOI: 10.1042/bj2680475
PubMed: 2163614
PubMed Central: PMC1131457
Affiliations:
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Kalyanaraman</name></author><author><name sortKey="Hammel, K E" sort="Hammel, K E" uniqKey="Hammel K" first="K E" last="Hammel">K E Hammel</name></author><author><name sortKey="Reinhammar, B" sort="Reinhammar, B" uniqKey="Reinhammar B" first="B" last="Reinhammar">B. Reinhammar</name></author><author><name sortKey="Kirk, T K" sort="Kirk, T K" uniqKey="Kirk T" first="T K" last="Kirk">T K Kirk</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1990">1990</date><idno type="RBID">pubmed:2163614</idno><idno type="pmid">2163614</idno><idno type="pmc">PMC1131457</idno><idno type="doi">10.1042/bj2680475</idno><idno type="wicri:Area/Main/Corpus">000F58</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000F58</idno><idno type="wicri:Area/Main/Curation">000F58</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000F58</idno><idno type="wicri:Area/Main/Exploration">000F58</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes.</title><author><name sortKey="Kersten, P J" sort="Kersten, P J" uniqKey="Kersten P" first="P J" last="Kersten">P J Kersten</name><affiliation wicri:level="2"><nlm:affiliation>Forest Products Laboratory, USDA Forest Service, Madison, WI 53705.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Wisconsin</region></placeName><wicri:cityArea>Forest Products Laboratory, USDA Forest Service, Madison</wicri:cityArea></affiliation></author><author><name sortKey="Kalyanaraman, B" sort="Kalyanaraman, B" uniqKey="Kalyanaraman B" first="B" last="Kalyanaraman">B. Kalyanaraman</name></author><author><name sortKey="Hammel, K E" sort="Hammel, K E" uniqKey="Hammel K" first="K E" last="Hammel">K E Hammel</name></author><author><name sortKey="Reinhammar, B" sort="Reinhammar, B" uniqKey="Reinhammar B" first="B" last="Reinhammar">B. Reinhammar</name></author><author><name sortKey="Kirk, T K" sort="Kirk, T K" uniqKey="Kirk T" first="T K" last="Kirk">T K Kirk</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="ISSN">0264-6021</idno><imprint><date when="1990" type="published">1990</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Benzene Derivatives (metabolism)</term><term>Chrysosporium (enzymology)</term><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Horseradish Peroxidase (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Kinetics (MeSH)</term><term>Laccase (MeSH)</term><term>Mitosporic Fungi (enzymology)</term><term>Oxidoreductases (metabolism)</term><term>Peroxidases (metabolism)</term><term>Spectrophotometry, Ultraviolet (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chrysosporium (enzymologie)</term><term>Cinétique (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Deuteromycota (enzymologie)</term><term>Dérivés du benzène (métabolisme)</term><term>Horseradish peroxidase (métabolisme)</term><term>Laccase (MeSH)</term><term>Oxidoreductases (métabolisme)</term><term>Peroxidases (métabolisme)</term><term>Spectrophotométrie UV (MeSH)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzene Derivatives</term><term>Horseradish Peroxidase</term><term>Oxidoreductases</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Chrysosporium</term><term>Deuteromycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Chrysosporium</term><term>Mitosporic Fungi</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Dérivés du benzène</term><term>Horseradish peroxidase</term><term>Oxidoreductases</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Spin Resonance Spectroscopy</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Laccase</term><term>Spectrophotometry, Ultraviolet</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Laccase</term><term>Spectrophotométrie UV</term><term>Spectroscopie de résonance de spin électronique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignin peroxidase oxidizes non-phenolic substrates by one electron to give aryl-cation-radical intermediates, which react further to give a variety of products. The present study investigated the possibility that other peroxidative and oxidative enzymes known to catalyse one-electron oxidations may also oxidize non-phenolics to cation-radical intermediates and that this ability is related to the redox potential of the substrate. Lignin peroxidase from the fungus Phanerochaete chrysosporium, horseradish peroxidase (HRP) and laccase from the fungus Trametes versicolor were chosen for investigation with methoxybenzenes as a homologous series of substrates. The twelve methoxybenzene congeners have known half-wave potentials that differ by as much as approximately 1 V. Lignin peroxidase oxidized the ten with the lowest half-wave potentials, whereas HRP oxidized the four lowest and laccase oxidized only 1,2,4,5-tetramethoxybenzene, the lowest. E.s.r. spectroscopy showed that this congener is oxidized to its cation radical by all three enzymes. Oxidation in each case gave the same products: 2,5-dimethoxy-p-benzoquinone and 4,5-dimethoxy-o-benzoquinone, in a 4:1 ratio, plus 2 mol of methanol for each 1 mol of substrate. Using HRP-catalysed oxidation, we showed that the quinone oxygen atoms are derived from water. We conclude that the three enzymes affect their substrates similarly, and that whether an aromatic compound is a substrate depends in large part on its redox potential. Furthermore, oxidized lignin peroxidase is clearly a stronger oxidant than oxidized HRP or laccase. Determination of the enzyme kinetic parameters for the methoxybenzene oxidations demonstrated further differences among the enzymes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2163614</PMID><DateCompleted><Year>1990</Year><Month>08</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0264-6021</ISSN><JournalIssue CitedMedium="Print"><Volume>268</Volume><Issue>2</Issue><PubDate><Year>1990</Year><Month>Jun</Month><Day>01</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes.</ArticleTitle><Pagination><MedlinePgn>475-80</MedlinePgn></Pagination><Abstract><AbstractText>Lignin peroxidase oxidizes non-phenolic substrates by one electron to give aryl-cation-radical intermediates, which react further to give a variety of products. The present study investigated the possibility that other peroxidative and oxidative enzymes known to catalyse one-electron oxidations may also oxidize non-phenolics to cation-radical intermediates and that this ability is related to the redox potential of the substrate. Lignin peroxidase from the fungus Phanerochaete chrysosporium, horseradish peroxidase (HRP) and laccase from the fungus Trametes versicolor were chosen for investigation with methoxybenzenes as a homologous series of substrates. The twelve methoxybenzene congeners have known half-wave potentials that differ by as much as approximately 1 V. Lignin peroxidase oxidized the ten with the lowest half-wave potentials, whereas HRP oxidized the four lowest and laccase oxidized only 1,2,4,5-tetramethoxybenzene, the lowest. E.s.r. spectroscopy showed that this congener is oxidized to its cation radical by all three enzymes. Oxidation in each case gave the same products: 2,5-dimethoxy-p-benzoquinone and 4,5-dimethoxy-o-benzoquinone, in a 4:1 ratio, plus 2 mol of methanol for each 1 mol of substrate. Using HRP-catalysed oxidation, we showed that the quinone oxygen atoms are derived from water. We conclude that the three enzymes affect their substrates similarly, and that whether an aromatic compound is a substrate depends in large part on its redox potential. Furthermore, oxidized lignin peroxidase is clearly a stronger oxidant than oxidized HRP or laccase. Determination of the enzyme kinetic parameters for the methoxybenzene oxidations demonstrated further differences among the enzymes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kersten</LastName><ForeName>P J</ForeName><Initials>PJ</Initials><AffiliationInfo><Affiliation>Forest Products Laboratory, USDA Forest Service, Madison, WI 53705.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kalyanaraman</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Hammel</LastName><ForeName>K E</ForeName><Initials>KE</Initials></Author><Author ValidYN="Y"><LastName>Reinhammar</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Kirk</LastName><ForeName>T K</ForeName><Initials>TK</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM-29035</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>RR-018008</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001555">Benzene Derivatives</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber><NameOfSubstance 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Kalyanaraman</name><name sortKey="Kirk, T K" sort="Kirk, T K" uniqKey="Kirk T" first="T K" last="Kirk">T K Kirk</name><name sortKey="Reinhammar, B" sort="Reinhammar, B" uniqKey="Reinhammar B" first="B" last="Reinhammar">B. Reinhammar</name></noCountry><country name="États-Unis"><region name="Wisconsin"><name sortKey="Kersten, P J" sort="Kersten, P J" uniqKey="Kersten P" first="P J" last="Kersten">P J Kersten</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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