NMR investigation of isotopically labeled cyanide derivatives of lignin peroxidase and manganese peroxidase.
Identifieur interne : 000D96 ( Main/Exploration ); précédent : 000D95; suivant : 000D97NMR investigation of isotopically labeled cyanide derivatives of lignin peroxidase and manganese peroxidase.
Auteurs : L. Banci [Italie] ; I. Bertini ; I C Kuan ; M. Tien ; P. Turano ; A J VilaSource :
- Biochemistry [ 0006-2960 ] ; 1993.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Cyanures, Histidine, Peroxidases.
- enzymologie : Basidiomycota.
- Deutérium, Spectroscopie par résonance magnétique, Structure moléculaire.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Cyanides, Histidine, Peroxidases.
- enzymology : Basidiomycota.
- chemical : Deuterium, Magnetic Resonance Spectroscopy, Molecular Structure.
Abstract
The 1H NMR spectroscopy was used to study lignin peroxidase (LiP) and manganese peroxidase (MnP) containing deuterated histidines. LiP and MnP were obtained from a histidine auxotroph of the fungus Phanerochaete chrysosporium grown in the presence of deuterated histidines. The derivatives with deuterated histidines have allowed a firm assignment of the protons of the distal and proximal histidines. We have also found that the LiP from this strain exhibits different orientations of the 2-vinyl group compared to the LiP from the strain previously studied. Mobility of the group has also been detected, thus explaining the apparent inconsistency between X-ray solid-state and NMR solution data. The 15N shift values of 15N-enriched CN- in the cyanide derivatives of LiP and MnP have also been measured. The shift patterns, both for 15N and for the proximal histidine protons of several peroxidases, are consistent with predominant contact shift contributions which reflect the bond strength of the metal-axial ligand. Finally, our results confirm a correlation between shift values of 15N and those of proximal histidine protons and the Fe3+/Fe2+ redox potentials.
DOI: 10.1021/bi00212a013
PubMed: 8257683
Affiliations:
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Tien</name></author><author><name sortKey="Turano, P" sort="Turano, P" uniqKey="Turano P" first="P" last="Turano">P. Turano</name></author><author><name sortKey="Vila, A J" sort="Vila, A J" uniqKey="Vila A" first="A J" last="Vila">A J Vila</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8257683</idno><idno type="pmid">8257683</idno><idno type="doi">10.1021/bi00212a013</idno><idno type="wicri:Area/Main/Corpus">000D75</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D75</idno><idno type="wicri:Area/Main/Curation">000D75</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D75</idno><idno type="wicri:Area/Main/Exploration">000D75</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">NMR investigation of isotopically labeled cyanide derivatives of lignin peroxidase and manganese peroxidase.</title><author><name sortKey="Banci, L" sort="Banci, L" uniqKey="Banci L" first="L" last="Banci">L. Banci</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence</wicri:regionArea><wicri:noRegion>University of Florence</wicri:noRegion></affiliation></author><author><name sortKey="Bertini, I" sort="Bertini, I" uniqKey="Bertini I" first="I" last="Bertini">I. Bertini</name></author><author><name sortKey="Kuan, I C" sort="Kuan, I C" uniqKey="Kuan I" first="I C" last="Kuan">I C Kuan</name></author><author><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></author><author><name sortKey="Turano, P" sort="Turano, P" uniqKey="Turano P" first="P" last="Turano">P. Turano</name></author><author><name sortKey="Vila, A J" sort="Vila, A J" uniqKey="Vila A" first="A J" last="Vila">A J Vila</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Cyanides (chemistry)</term><term>Deuterium (MeSH)</term><term>Histidine (chemistry)</term><term>Magnetic Resonance Spectroscopy (MeSH)</term><term>Molecular Structure (MeSH)</term><term>Peroxidases (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term><term>Cyanures (composition chimique)</term><term>Deutérium (MeSH)</term><term>Histidine (composition chimique)</term><term>Peroxidases (composition chimique)</term><term>Spectroscopie par résonance magnétique (MeSH)</term><term>Structure moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cyanides</term><term>Histidine</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cyanures</term><term>Histidine</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" type="chemical" xml:lang="en"><term>Deuterium</term><term>Magnetic Resonance Spectroscopy</term><term>Molecular Structure</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Deutérium</term><term>Spectroscopie par résonance magnétique</term><term>Structure moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The 1H NMR spectroscopy was used to study lignin peroxidase (LiP) and manganese peroxidase (MnP) containing deuterated histidines. LiP and MnP were obtained from a histidine auxotroph of the fungus Phanerochaete chrysosporium grown in the presence of deuterated histidines. The derivatives with deuterated histidines have allowed a firm assignment of the protons of the distal and proximal histidines. We have also found that the LiP from this strain exhibits different orientations of the 2-vinyl group compared to the LiP from the strain previously studied. Mobility of the group has also been detected, thus explaining the apparent inconsistency between X-ray solid-state and NMR solution data. The 15N shift values of 15N-enriched CN- in the cyanide derivatives of LiP and MnP have also been measured. The shift patterns, both for 15N and for the proximal histidine protons of several peroxidases, are consistent with predominant contact shift contributions which reflect the bond strength of the metal-axial ligand. Finally, our results confirm a correlation between shift values of 15N and those of proximal histidine protons and the Fe3+/Fe2+ redox potentials.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8257683</PMID><DateCompleted><Year>1994</Year><Month>01</Month><Day>19</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>32</Volume><Issue>49</Issue><PubDate><Year>1993</Year><Month>Dec</Month><Day>14</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>NMR investigation of isotopically labeled cyanide derivatives of lignin peroxidase and manganese peroxidase.</ArticleTitle><Pagination><MedlinePgn>13483-9</MedlinePgn></Pagination><Abstract><AbstractText>The 1H NMR spectroscopy was used to study lignin peroxidase (LiP) and manganese peroxidase (MnP) containing deuterated histidines. LiP and MnP were obtained from a histidine auxotroph of the fungus Phanerochaete chrysosporium grown in the presence of deuterated histidines. The derivatives with deuterated histidines have allowed a firm assignment of the protons of the distal and proximal histidines. We have also found that the LiP from this strain exhibits different orientations of the 2-vinyl group compared to the LiP from the strain previously studied. Mobility of the group has also been detected, thus explaining the apparent inconsistency between X-ray solid-state and NMR solution data. The 15N shift values of 15N-enriched CN- in the cyanide derivatives of LiP and MnP have also been measured. The shift patterns, both for 15N and for the proximal histidine protons of several peroxidases, are consistent with predominant contact shift contributions which reflect the bond strength of the metal-axial ligand. Finally, our results confirm a correlation between shift values of 15N and those of proximal histidine protons and the Fe3+/Fe2+ redox potentials.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Banci</LastName><ForeName>L</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bertini</LastName><ForeName>I</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Kuan</LastName><ForeName>I C</ForeName><Initials>IC</Initials></Author><Author ValidYN="Y"><LastName>Tien</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Turano</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Vila</LastName><ForeName>A J</ForeName><Initials>AJ</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="D003486">Cyanides</NameOfSubstance></Chemical><Chemical><RegistryNumber>4QD397987E</RegistryNumber><NameOfSubstance UI="D006639">Histidine</NameOfSubstance></Chemical><Chemical><RegistryNumber>AR09D82C7G</RegistryNumber><NameOfSubstance UI="D003903">Deuterium</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>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese 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="D003486" MajorTopicYN="N">Cyanides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003903" MajorTopicYN="N">Deuterium</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006639" MajorTopicYN="N">Histidine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="Y">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>12</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>12</Month><Day>14</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>12</Month><Day>14</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8257683</ArticleId><ArticleId IdType="doi">10.1021/bi00212a013</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><noCountry><name sortKey="Bertini, I" sort="Bertini, I" uniqKey="Bertini I" first="I" last="Bertini">I. Bertini</name><name sortKey="Kuan, I C" sort="Kuan, I C" uniqKey="Kuan I" first="I C" last="Kuan">I C Kuan</name><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name><name sortKey="Turano, P" sort="Turano, P" uniqKey="Turano P" first="P" last="Turano">P. Turano</name><name sortKey="Vila, A J" sort="Vila, A J" uniqKey="Vila A" first="A J" last="Vila">A J Vila</name></noCountry><country name="Italie"><noRegion><name sortKey="Banci, L" sort="Banci, L" uniqKey="Banci L" first="L" last="Banci">L. Banci</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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