EPR detection and characterization of lignin peroxidase porphyrin pi-cation radical.
Identifieur interne : 000C55 ( Main/Exploration ); précédent : 000C54; suivant : 000C56EPR detection and characterization of lignin peroxidase porphyrin pi-cation radical.
Auteurs : A. Khindaria [États-Unis] ; S D AustSource :
- Biochemistry [ 0006-2960 ] ; 1996.
Descripteurs français
- KwdFr :
- Basidiomycota (enzymologie), Cations (MeSH), Composés du fer III (composition chimique), Hème (composition chimique), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxyde d'hydrogène (métabolisme), Porphyrines (composition chimique), Radicaux libres (MeSH), Spectroscopie de résonance de spin électronique (MeSH), Température (MeSH).
- MESH :
- composition chimique : Composés du fer III, Hème, Peroxidases, Porphyrines.
- enzymologie : Basidiomycota.
- métabolisme : Peroxyde d'hydrogène.
- Cations, Oxydoréduction, Radicaux libres, Spectroscopie de résonance de spin électronique, Température.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Ferric Compounds, Heme, Peroxidases, Porphyrins.
- chemical , metabolism : Hydrogen Peroxide.
- chemical : Cations, Free Radicals.
- enzymology : Basidiomycota.
- Electron Spin Resonance Spectroscopy, Oxidation-Reduction, Temperature.
Abstract
Lignin peroxidase (LiP) from Phanerochaete chrysosporium catalyzes the H2O2 dependent one- and two-electron oxidations of substrates. The catalytic cycle involves the oxidation of ferric-LiP by H2O2 by two electrons to compound I, which is an oxoferryl heme and a free radical. It has been speculated that the unpaired electron is in a pi delocalized porphyrin radical. However, no direct evidence for the presence of the free radical has been reported. We present electron paramagnetic resonance (EPR) detection and characterization of compound I of LiP. The LiP compound I EPR signal is different than those reported previously for compound I of horseradish peroxidase and chloroperoxidase. However, the EPR signal of compound I of LiP (axial g tensor extending from gperpendicular = 3.42 to gparallel approximately 2) is very similar to the EPR signals of compound I of ascorbate peroxidase and catalase from Micrococcus lysodeikticus, in which the radical has been identified as a porphyrin pi-cation radical. On the basis of the analysis of our data and comparison with the earlier published results for compounds I of other peroxidases, we interpret the LiP compound I signal by a model for exchange coupling between an S = 1 oxyferryl [Fe = O]2+ moiety and a porphyrin pi-cation radical (S = 1/2) [Schulz, C.E., et al. (1979) FEBS Lett. 103, 102-105]. The exchange coupling is characterized by ferromagnetic rather than an antiferromagnetic interaction between the two species. The ferric-Lip EPR signal suggests that the iron in the heme is in near perfect orthogonal symmetry and provides additional evidence of the ferromagnetic interaction between the oxoferryl iron center and the porphyrin pi-cation radical.
DOI: 10.1021/bi961297+
PubMed: 8855947
Affiliations:
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Khindaria</name><affiliation wicri:level="1"><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4705, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biotechnology Center, Utah State University, Logan 84322-4705</wicri:regionArea><wicri:noRegion>Logan 84322-4705</wicri:noRegion></affiliation></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="1996">1996</date><idno type="RBID">pubmed:8855947</idno><idno type="pmid">8855947</idno><idno type="doi">10.1021/bi961297+</idno><idno type="wicri:Area/Main/Corpus">000C31</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C31</idno><idno type="wicri:Area/Main/Curation">000C31</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C31</idno><idno type="wicri:Area/Main/Exploration">000C31</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">EPR detection and characterization of lignin peroxidase porphyrin pi-cation radical.</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 84322-4705, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biotechnology Center, Utah State University, Logan 84322-4705</wicri:regionArea><wicri:noRegion>Logan 84322-4705</wicri:noRegion></affiliation></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="1996" type="published">1996</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Cations (MeSH)</term><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Ferric Compounds (chemistry)</term><term>Free Radicals (MeSH)</term><term>Heme (chemistry)</term><term>Hydrogen Peroxide (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Porphyrins (chemistry)</term><term>Temperature (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term><term>Cations (MeSH)</term><term>Composés du fer III (composition chimique)</term><term>Hème (composition chimique)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (composition chimique)</term><term>Peroxyde d'hydrogène (métabolisme)</term><term>Porphyrines (composition chimique)</term><term>Radicaux libres (MeSH)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term><term>Température (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ferric Compounds</term><term>Heme</term><term>Peroxidases</term><term>Porphyrins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hydrogen Peroxide</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cations</term><term>Free Radicals</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Composés du fer III</term><term>Hème</term><term>Peroxidases</term><term>Porphyrines</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>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Spin Resonance Spectroscopy</term><term>Oxidation-Reduction</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cations</term><term>Oxydoréduction</term><term>Radicaux libres</term><term>Spectroscopie de résonance de spin électronique</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignin peroxidase (LiP) from Phanerochaete chrysosporium catalyzes the H2O2 dependent one- and two-electron oxidations of substrates. The catalytic cycle involves the oxidation of ferric-LiP by H2O2 by two electrons to compound I, which is an oxoferryl heme and a free radical. It has been speculated that the unpaired electron is in a pi delocalized porphyrin radical. However, no direct evidence for the presence of the free radical has been reported. We present electron paramagnetic resonance (EPR) detection and characterization of compound I of LiP. The LiP compound I EPR signal is different than those reported previously for compound I of horseradish peroxidase and chloroperoxidase. However, the EPR signal of compound I of LiP (axial g tensor extending from gperpendicular = 3.42 to gparallel approximately 2) is very similar to the EPR signals of compound I of ascorbate peroxidase and catalase from Micrococcus lysodeikticus, in which the radical has been identified as a porphyrin pi-cation radical. On the basis of the analysis of our data and comparison with the earlier published results for compounds I of other peroxidases, we interpret the LiP compound I signal by a model for exchange coupling between an S = 1 oxyferryl [Fe = O]2+ moiety and a porphyrin pi-cation radical (S = 1/2) [Schulz, C.E., et al. (1979) FEBS Lett. 103, 102-105]. The exchange coupling is characterized by ferromagnetic rather than an antiferromagnetic interaction between the two species. The ferric-Lip EPR signal suggests that the iron in the heme is in near perfect orthogonal symmetry and provides additional evidence of the ferromagnetic interaction between the oxoferryl iron center and the porphyrin pi-cation radical.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8855947</PMID><DateCompleted><Year>1996</Year><Month>11</Month><Day>27</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>35</Volume><Issue>40</Issue><PubDate><Year>1996</Year><Month>Oct</Month><Day>08</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>EPR detection and characterization of lignin peroxidase porphyrin pi-cation radical.</ArticleTitle><Pagination><MedlinePgn>13107-11</MedlinePgn></Pagination><Abstract><AbstractText>Lignin peroxidase (LiP) from Phanerochaete chrysosporium catalyzes the H2O2 dependent one- and two-electron oxidations of substrates. The catalytic cycle involves the oxidation of ferric-LiP by H2O2 by two electrons to compound I, which is an oxoferryl heme and a free radical. It has been speculated that the unpaired electron is in a pi delocalized porphyrin radical. However, no direct evidence for the presence of the free radical has been reported. We present electron paramagnetic resonance (EPR) detection and characterization of compound I of LiP. The LiP compound I EPR signal is different than those reported previously for compound I of horseradish peroxidase and chloroperoxidase. However, the EPR signal of compound I of LiP (axial g tensor extending from gperpendicular = 3.42 to gparallel approximately 2) is very similar to the EPR signals of compound I of ascorbate peroxidase and catalase from Micrococcus lysodeikticus, in which the radical has been identified as a porphyrin pi-cation radical. On the basis of the analysis of our data and comparison with the earlier published results for compounds I of other peroxidases, we interpret the LiP compound I signal by a model for exchange coupling between an S = 1 oxyferryl [Fe = O]2+ moiety and a porphyrin pi-cation radical (S = 1/2) [Schulz, C.E., et al. (1979) FEBS Lett. 103, 102-105]. The exchange coupling is characterized by ferromagnetic rather than an antiferromagnetic interaction between the two species. The ferric-Lip EPR signal suggests that the iron in the heme is in near perfect orthogonal symmetry and provides additional evidence of the ferromagnetic interaction between the oxoferryl iron center and the porphyrin pi-cation radical.</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 84322-4705, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aust</LastName><ForeName>S D</ForeName><Initials>SD</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>ESO4922</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, 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="D002412">Cations</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005290">Ferric Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005609">Free Radicals</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011166">Porphyrins</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</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="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002412" MajorTopicYN="N">Cations</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005290" MajorTopicYN="N">Ferric Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005609" MajorTopicYN="N">Free Radicals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011166" MajorTopicYN="N">Porphyrins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>10</Month><Day>8</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1996</Year><Month>10</Month><Day>8</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>10</Month><Day>8</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8855947</ArticleId><ArticleId IdType="doi">10.1021/bi961297+</ArticleId><ArticleId IdType="pii">bi961297+</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></noCountry><country name="États-Unis"><noRegion><name sortKey="Khindaria, A" sort="Khindaria, A" uniqKey="Khindaria A" first="A" last="Khindaria">A. 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