Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex.
Identifieur interne : 000C16 ( Main/Exploration ); précédent : 000C15; suivant : 000C17Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex.
Auteurs : A. Khindaria [États-Unis] ; G. Nie ; S D AustSource :
- Biochemistry [ 0006-2960 ] ; 1997.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Basidiomycota.
- métabolisme : Alcools benzyliques, Hémoprotéines, Isoenzymes, Peroxidases.
- Basse température, Cations, Radicaux libres, Spectroscopie de résonance de spin électronique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Benzyl Alcohols, Hemeproteins, Isoenzymes, Peroxidases.
- enzymology : Basidiomycota.
- chemical : Cations, Cold Temperature, Electron Spin Resonance Spectroscopy, Free Radicals.
Abstract
Lignin peroxidases (LiP) from the white-rot fungus Phanerochaete chrysosporium oxidize veratryl alcohol (VA) by two electrons to veratryl aldehyde, although the VA cation radical (VA.+) is an intermediate [Khindaria, A., et al. (1995) Biochemistry 34, 6020-6025]. It was speculated, on the basis of kinetic evidence, that VA*+ can form a catalytic complex with LiP compound II. We have used low-temperature EPR to provide direct evidence for the formation of the complex. The EPR spectrum of VA*+ obtained at 4 K was explained by a model for coupling between the oxoferryl moiety of the heme (S = 1) and VA.+ (S = 1/2) similar to the model proposed for an oxyferryl and a porphyrin pi cation radical of horseradish peroxidase. The coupling constant suggested that VA.+ was equally ferro- and antiferromagnetically coupled to the oxoferryl moiety. The spectrum was simulated with g perpendicular only marginally greater than g parallel. This was surprising since the only other known organic radical coupled to the heme iron in a peroxidase is the tryptophan cation radical in cytochrome c peroxidase which exhibits a g tensor with g parallel greater than g perpendicular. Spin concentration analysis suggested that the 1 mol of VA*+ was coupled to the oxoferryl moiety per mole of enzyme. The VA.+ signal decayed with a first-order decay constant of 1.76 s-1, in close agreement with the earlier published decay constant of 1.85 s-1 from room-temperature EPR studies. The exchange coupling between VA.+ and the oxoferryl moiety strongly advocates calling this species (VA.+ and LiP compound II) a catalytic complex.
DOI: 10.1021/bi9715730
PubMed: 9369491
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex.</title><author><name sortKey="Khindaria, A" sort="Khindaria, A" uniqKey="Khindaria A" first="A" last="Khindaria">A. Khindaria</name><affiliation wicri:level="1"><nlm:affiliation>Biotechnology Center, Utah State University, Logan, Utah 84322-4705, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biotechnology Center, Utah State University, Logan, Utah 84322-4705</wicri:regionArea><wicri:noRegion>Utah 84322-4705</wicri:noRegion></affiliation></author><author><name sortKey="Nie, G" sort="Nie, G" uniqKey="Nie G" first="G" last="Nie">G. Nie</name></author><author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1997">1997</date><idno type="RBID">pubmed:9369491</idno><idno type="pmid">9369491</idno><idno type="doi">10.1021/bi9715730</idno><idno type="wicri:Area/Main/Corpus">000B95</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B95</idno><idno type="wicri:Area/Main/Curation">000B95</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000B95</idno><idno type="wicri:Area/Main/Exploration">000B95</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex.</title><author><name sortKey="Khindaria, A" sort="Khindaria, A" uniqKey="Khindaria A" first="A" last="Khindaria">A. Khindaria</name><affiliation wicri:level="1"><nlm:affiliation>Biotechnology Center, Utah State University, Logan, Utah 84322-4705, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biotechnology Center, Utah State University, Logan, Utah 84322-4705</wicri:regionArea><wicri:noRegion>Utah 84322-4705</wicri:noRegion></affiliation></author><author><name sortKey="Nie, G" sort="Nie, G" uniqKey="Nie G" first="G" last="Nie">G. Nie</name></author><author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Benzyl Alcohols (metabolism)</term><term>Cations (MeSH)</term><term>Cold Temperature (MeSH)</term><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Free Radicals (MeSH)</term><term>Hemeproteins (metabolism)</term><term>Isoenzymes (metabolism)</term><term>Peroxidases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcools benzyliques (métabolisme)</term><term>Basidiomycota (enzymologie)</term><term>Basse température (MeSH)</term><term>Cations (MeSH)</term><term>Hémoprotéines (métabolisme)</term><term>Isoenzymes (métabolisme)</term><term>Peroxidases (métabolisme)</term><term>Radicaux libres (MeSH)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzyl Alcohols</term><term>Hemeproteins</term><term>Isoenzymes</term><term>Peroxidases</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>Alcools benzyliques</term><term>Hémoprotéines</term><term>Isoenzymes</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cations</term><term>Cold Temperature</term><term>Electron Spin Resonance Spectroscopy</term><term>Free Radicals</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Basse température</term><term>Cations</term><term>Radicaux libres</term><term>Spectroscopie de résonance de spin électronique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignin peroxidases (LiP) from the white-rot fungus Phanerochaete chrysosporium oxidize veratryl alcohol (VA) by two electrons to veratryl aldehyde, although the VA cation radical (VA.+) is an intermediate [Khindaria, A., et al. (1995) Biochemistry 34, 6020-6025]. It was speculated, on the basis of kinetic evidence, that VA*+ can form a catalytic complex with LiP compound II. We have used low-temperature EPR to provide direct evidence for the formation of the complex. The EPR spectrum of VA*+ obtained at 4 K was explained by a model for coupling between the oxoferryl moiety of the heme (S = 1) and VA.+ (S = 1/2) similar to the model proposed for an oxyferryl and a porphyrin pi cation radical of horseradish peroxidase. The coupling constant suggested that VA.+ was equally ferro- and antiferromagnetically coupled to the oxoferryl moiety. The spectrum was simulated with g perpendicular only marginally greater than g parallel. This was surprising since the only other known organic radical coupled to the heme iron in a peroxidase is the tryptophan cation radical in cytochrome c peroxidase which exhibits a g tensor with g parallel greater than g perpendicular. Spin concentration analysis suggested that the 1 mol of VA*+ was coupled to the oxoferryl moiety per mole of enzyme. The VA.+ signal decayed with a first-order decay constant of 1.76 s-1, in close agreement with the earlier published decay constant of 1.85 s-1 from room-temperature EPR studies. The exchange coupling between VA.+ and the oxoferryl moiety strongly advocates calling this species (VA.+ and LiP compound II) a catalytic complex.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9369491</PMID><DateCompleted><Year>1997</Year><Month>12</Month><Day>19</Day></DateCompleted><DateRevised><Year>2012</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>36</Volume><Issue>46</Issue><PubDate><Year>1997</Year><Month>Nov</Month><Day>18</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex.</ArticleTitle><Pagination><MedlinePgn>14181-5</MedlinePgn></Pagination><Abstract><AbstractText>Lignin peroxidases (LiP) from the white-rot fungus Phanerochaete chrysosporium oxidize veratryl alcohol (VA) by two electrons to veratryl aldehyde, although the VA cation radical (VA.+) is an intermediate [Khindaria, A., et al. (1995) Biochemistry 34, 6020-6025]. It was speculated, on the basis of kinetic evidence, that VA*+ can form a catalytic complex with LiP compound II. We have used low-temperature EPR to provide direct evidence for the formation of the complex. The EPR spectrum of VA*+ obtained at 4 K was explained by a model for coupling between the oxoferryl moiety of the heme (S = 1) and VA.+ (S = 1/2) similar to the model proposed for an oxyferryl and a porphyrin pi cation radical of horseradish peroxidase. The coupling constant suggested that VA.+ was equally ferro- and antiferromagnetically coupled to the oxoferryl moiety. The spectrum was simulated with g perpendicular only marginally greater than g parallel. This was surprising since the only other known organic radical coupled to the heme iron in a peroxidase is the tryptophan cation radical in cytochrome c peroxidase which exhibits a g tensor with g parallel greater than g perpendicular. Spin concentration analysis suggested that the 1 mol of VA*+ was coupled to the oxoferryl moiety per mole of enzyme. The VA.+ signal decayed with a first-order decay constant of 1.76 s-1, in close agreement with the earlier published decay constant of 1.85 s-1 from room-temperature EPR studies. The exchange coupling between VA.+ and the oxoferryl moiety strongly advocates calling this species (VA.+ and LiP compound II) a catalytic complex.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Khindaria</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Biotechnology Center, Utah State University, Logan, Utah 84322-4705, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nie</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Aust</LastName><ForeName>S D</ForeName><Initials>SD</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</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="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002412">Cations</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005609">Free Radicals</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006420">Hemeproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</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><Chemical><RegistryNumber>MB4T4A711H</RegistryNumber><NameOfSubstance UI="C042197">veratryl alcohol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><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><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002412" MajorTopicYN="N">Cations</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003080" MajorTopicYN="N">Cold Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005609" MajorTopicYN="N">Free Radicals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006420" MajorTopicYN="N">Hemeproteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>12</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>12</Month><Day>31</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>12</Month><Day>31</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9369491</ArticleId><ArticleId IdType="doi">10.1021/bi9715730</ArticleId><ArticleId IdType="pii">bi9715730</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name><name sortKey="Nie, G" sort="Nie, G" uniqKey="Nie G" first="G" last="Nie">G. Nie</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Khindaria, A" sort="Khindaria, A" uniqKey="Khindaria A" first="A" last="Khindaria">A. Khindaria</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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