X-ray absorption spectroscopy comparison of the active site structures of Phanerochaete chrysosporium lignin peroxidase isoenzymes H2, H3, H4, H5, H8, and H10.
Identifieur interne : 000C72 ( Main/Exploration ); précédent : 000C71; suivant : 000C73X-ray absorption spectroscopy comparison of the active site structures of Phanerochaete chrysosporium lignin peroxidase isoenzymes H2, H3, H4, H5, H8, and H10.
Auteurs : R. Sinclair [États-Unis] ; B. Copeland ; I. Yamazaki ; L. PowersSource :
- Biochemistry [ 0006-2960 ] ; 1995.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Hème, Isoenzymes, Manganèse, Peroxidases.
- enzymologie : Champignons.
- méthodes : Analyse spectrale.
- Analyse de Fourier, Rayons X, Sites de fixation.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Heme, Isoenzymes, Manganese, Peroxidases.
- enzymology : Fungi.
- methods : Spectrum Analysis.
- Binding Sites, Fourier Analysis, X-Rays.
Abstract
The iron heme and its immediate environment can provide information that is pivotal to our understanding of the structural and mechanistic features that confer unusual properties to the heme peroxidases. X-ray absorption spectroscopy (XAS), which is ideally suited for the investigation of the local environment and electronic structure of the heme iron of hemeproteins, has been used to characterize a variety of lignin peroxidase and manganese-dependent peroxidase isoenzymes produced by the white rot fungus Phanerochaete chrysosporium. The data suggest no differences within the error in the first coordination shell of iron for the isoenzymes H2, H3, H4, H5, H8, and H10 examined in this study. The pyrrole nitrogens are at a distance of 2.05 +/- 0.015 A, and the proximal histidine nitrogens are at 1.93 +/- 0.02 A, while the sixth ligands are located at 2.17 +/- 0.03 A. Significant differences are observed in higher coordination shells which may be related to conformational differences in the heme.
DOI: 10.1021/bi00040a032
PubMed: 7548080
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Yamazaki</name></author><author><name sortKey="Powers, L" sort="Powers, L" uniqKey="Powers L" first="L" last="Powers">L. Powers</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1995">1995</date><idno type="RBID">pubmed:7548080</idno><idno type="pmid">7548080</idno><idno type="doi">10.1021/bi00040a032</idno><idno type="wicri:Area/Main/Corpus">000C79</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C79</idno><idno type="wicri:Area/Main/Curation">000C79</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C79</idno><idno type="wicri:Area/Main/Exploration">000C79</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">X-ray absorption spectroscopy comparison of the active site structures of Phanerochaete chrysosporium lignin peroxidase isoenzymes H2, H3, H4, H5, H8, and H10.</title><author><name sortKey="Sinclair, R" sort="Sinclair, R" uniqKey="Sinclair R" first="R" last="Sinclair">R. Sinclair</name><affiliation wicri:level="1"><nlm:affiliation>National Center for the Design of Molecular Function, Utah State University, Logan 84322-4630, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>National Center for the Design of Molecular Function, Utah State University, Logan 84322-4630</wicri:regionArea><wicri:noRegion>Logan 84322-4630</wicri:noRegion></affiliation></author><author><name sortKey="Copeland, B" sort="Copeland, B" uniqKey="Copeland B" first="B" last="Copeland">B. Copeland</name></author><author><name sortKey="Yamazaki, I" sort="Yamazaki, I" uniqKey="Yamazaki I" first="I" last="Yamazaki">I. Yamazaki</name></author><author><name sortKey="Powers, L" sort="Powers, L" uniqKey="Powers L" first="L" last="Powers">L. Powers</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>Binding Sites (MeSH)</term><term>Fourier Analysis (MeSH)</term><term>Fungi (enzymology)</term><term>Heme (chemistry)</term><term>Isoenzymes (chemistry)</term><term>Manganese (chemistry)</term><term>Peroxidases (chemistry)</term><term>Spectrum Analysis (methods)</term><term>X-Rays (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de Fourier (MeSH)</term><term>Analyse spectrale (méthodes)</term><term>Champignons (enzymologie)</term><term>Hème (composition chimique)</term><term>Isoenzymes (composition chimique)</term><term>Manganèse (composition chimique)</term><term>Peroxidases (composition chimique)</term><term>Rayons X (MeSH)</term><term>Sites de fixation (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Heme</term><term>Isoenzymes</term><term>Manganese</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Hème</term><term>Isoenzymes</term><term>Manganèse</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Champignons</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Spectrum Analysis</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Analyse spectrale</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Fourier Analysis</term><term>X-Rays</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de Fourier</term><term>Rayons X</term><term>Sites de fixation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The iron heme and its immediate environment can provide information that is pivotal to our understanding of the structural and mechanistic features that confer unusual properties to the heme peroxidases. X-ray absorption spectroscopy (XAS), which is ideally suited for the investigation of the local environment and electronic structure of the heme iron of hemeproteins, has been used to characterize a variety of lignin peroxidase and manganese-dependent peroxidase isoenzymes produced by the white rot fungus Phanerochaete chrysosporium. The data suggest no differences within the error in the first coordination shell of iron for the isoenzymes H2, H3, H4, H5, H8, and H10 examined in this study. The pyrrole nitrogens are at a distance of 2.05 +/- 0.015 A, and the proximal histidine nitrogens are at 1.93 +/- 0.02 A, while the sixth ligands are located at 2.17 +/- 0.03 A. Significant differences are observed in higher coordination shells which may be related to conformational differences in the heme.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7548080</PMID><DateCompleted><Year>1995</Year><Month>11</Month><Day>09</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>40</Issue><PubDate><Year>1995</Year><Month>Oct</Month><Day>10</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>X-ray absorption spectroscopy comparison of the active site structures of Phanerochaete chrysosporium lignin peroxidase isoenzymes H2, H3, H4, H5, H8, and H10.</ArticleTitle><Pagination><MedlinePgn>13176-82</MedlinePgn></Pagination><Abstract><AbstractText>The iron heme and its immediate environment can provide information that is pivotal to our understanding of the structural and mechanistic features that confer unusual properties to the heme peroxidases. X-ray absorption spectroscopy (XAS), which is ideally suited for the investigation of the local environment and electronic structure of the heme iron of hemeproteins, has been used to characterize a variety of lignin peroxidase and manganese-dependent peroxidase isoenzymes produced by the white rot fungus Phanerochaete chrysosporium. The data suggest no differences within the error in the first coordination shell of iron for the isoenzymes H2, H3, H4, H5, H8, and H10 examined in this study. The pyrrole nitrogens are at a distance of 2.05 +/- 0.015 A, and the proximal histidine nitrogens are at 1.93 +/- 0.02 A, while the sixth ligands are located at 2.17 +/- 0.03 A. Significant differences are observed in higher coordination shells which may be related to conformational differences in the heme.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sinclair</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>National Center for the Design of Molecular Function, Utah State University, Logan 84322-4630, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Copeland</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Yamazaki</LastName><ForeName>I</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Powers</LastName><ForeName>L</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>ES-04922</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>RR-01633</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</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="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber><NameOfSubstance UI="D008345">Manganese</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="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005583" MajorTopicYN="N">Fourier Analysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013057" MajorTopicYN="N">Spectrum Analysis</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014965" MajorTopicYN="N">X-Rays</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1995</Year><Month>10</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1995</Year><Month>10</Month><Day>10</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1995</Year><Month>10</Month><Day>10</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7548080</ArticleId><ArticleId IdType="doi">10.1021/bi00040a032</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Copeland, B" sort="Copeland, B" uniqKey="Copeland B" first="B" last="Copeland">B. Copeland</name><name sortKey="Powers, L" sort="Powers, L" uniqKey="Powers L" first="L" last="Powers">L. Powers</name><name sortKey="Yamazaki, I" sort="Yamazaki, I" uniqKey="Yamazaki I" first="I" last="Yamazaki">I. Yamazaki</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Sinclair, R" sort="Sinclair, R" uniqKey="Sinclair R" first="R" last="Sinclair">R. Sinclair</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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