Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes.
Identifieur interne : 000222 ( Main/Exploration ); précédent : 000221; suivant : 000223Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes.
Auteurs : Francesca Camponeschi [Italie] ; Riccardo Muzzioli [Italie] ; Simone Ciofi-Baffoni [Italie] ; Mario Piccioli [Italie] ; Lucia Banci [Italie]Source :
- Journal of molecular biology [ 1089-8638 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Ferrosulfoprotéines.
- métabolisme : Adémétionine, Fer, Ferrosulfoprotéines.
- méthodes : Spectroscopie par résonance magnétique.
- Catalyse, Spectroscopie de résonance de spin électronique, Transport d'électrons.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Iron-Sulfur Proteins.
- chemical , metabolism : Iron, Iron-Sulfur Proteins, S-Adenosylmethionine.
- methods : Magnetic Resonance Spectroscopy.
- Catalysis, Electron Spin Resonance Spectroscopy, Electron Transport.
Abstract
Iron-sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes.
DOI: 10.1016/j.jmb.2019.08.018
PubMed: 31493409
Affiliations:
Links toward previous steps (curation, corpus...)
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Electronic address: banci@cerm.unifi.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy; Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="eISSN">1089-8638</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Catalysis (MeSH)</term><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Electron Transport (MeSH)</term><term>Iron (metabolism)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Magnetic Resonance Spectroscopy (methods)</term><term>S-Adenosylmethionine (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adémétionine (métabolisme)</term><term>Catalyse (MeSH)</term><term>Fer (métabolisme)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term><term>Spectroscopie par résonance magnétique (méthodes)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Iron</term><term>Iron-Sulfur Proteins</term><term>S-Adenosylmethionine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Ferrosulfoprotéines</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Magnetic Resonance Spectroscopy</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adémétionine</term><term>Fer</term><term>Ferrosulfoprotéines</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Spectroscopie par résonance magnétique</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Electron Spin Resonance Spectroscopy</term><term>Electron Transport</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Spectroscopie de résonance de spin électronique</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Iron-sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that <sup>1</sup>H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. <sup>1</sup>H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31493409</PMID><DateCompleted><Year>2020</Year><Month>06</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>06</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1089-8638</ISSN><JournalIssue CitedMedium="Internet"><Volume>431</Volume><Issue>22</Issue><PubDate><Year>2019</Year><Month>11</Month><Day>08</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Paramagnetic <sup>1</sup>H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes.</ArticleTitle><Pagination><MedlinePgn>4514-4522</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0022-2836(19)30542-X</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jmb.2019.08.018</ELocationID><Abstract><AbstractText>Iron-sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that <sup>1</sup>H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. <sup>1</sup>H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes.</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Camponeschi</LastName><ForeName>Francesca</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy; Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Muzzioli</LastName><ForeName>Riccardo</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy; Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ciofi-Baffoni</LastName><ForeName>Simone</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy; Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Piccioli</LastName><ForeName>Mario</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy; Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Banci</LastName><ForeName>Lucia</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy; Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy. Electronic address: banci@cerm.unifi.it.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>09</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mol Biol</MedlineTA><NlmUniqueID>2985088R</NlmUniqueID><ISSNLinking>0022-2836</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>7LP2MPO46S</RegistryNumber><NameOfSubstance UI="D012436">S-Adenosylmethionine</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012436" MajorTopicYN="N">S-Adenosylmethionine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Electron transfer</Keyword><Keyword MajorTopicYN="Y">Enzyme mechanism</Keyword><Keyword MajorTopicYN="Y">Iron–sulfur proteins</Keyword><Keyword MajorTopicYN="Y">Lipoyl synthase</Keyword><Keyword MajorTopicYN="Y">Metallo enzyme</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>07</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>08</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>08</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>9</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>6</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>9</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31493409</ArticleId><ArticleId IdType="pii">S0022-2836(19)30542-X</ArticleId><ArticleId IdType="doi">10.1016/j.jmb.2019.08.018</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><country name="Italie"><noRegion><name sortKey="Camponeschi, Francesca" sort="Camponeschi, Francesca" uniqKey="Camponeschi F" first="Francesca" last="Camponeschi">Francesca Camponeschi</name></noRegion><name sortKey="Banci, Lucia" sort="Banci, Lucia" uniqKey="Banci L" first="Lucia" last="Banci">Lucia Banci</name><name sortKey="Ciofi Baffoni, Simone" sort="Ciofi Baffoni, Simone" uniqKey="Ciofi Baffoni S" first="Simone" last="Ciofi-Baffoni">Simone Ciofi-Baffoni</name><name sortKey="Muzzioli, Riccardo" sort="Muzzioli, Riccardo" uniqKey="Muzzioli R" first="Riccardo" last="Muzzioli">Riccardo Muzzioli</name><name sortKey="Piccioli, Mario" sort="Piccioli, Mario" uniqKey="Piccioli M" first="Mario" last="Piccioli">Mario Piccioli</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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