Measuring transverse relaxation in highly paramagnetic systems.
Identifieur interne : 000082 ( Main/Exploration ); précédent : 000081; suivant : 000083Measuring transverse relaxation in highly paramagnetic systems.
Auteurs : Michele Invernici [Italie] ; Inês B. Trindade [Portugal] ; Francesca Cantini [Italie] ; Ricardo O. Louro [Portugal] ; Mario Piccioli [Italie]Source :
- Journal of biomolecular NMR [ 1573-5001 ] ; 2020.
Abstract
The enhancement of nuclear relaxation rates due to the interaction with a paramagnetic center (known as Paramagnetic Relaxation Enhancement) is a powerful source of structural and dynamics information, widely used in structural biology. However, many signals affected by the hyperfine interaction relax faster than the evolution periods of common NMR experiments and therefore they are broadened beyond detection. This gives rise to a so-called blind sphere around the paramagnetic center, which is a major limitation in the use of PREs. Reducing the blind sphere is extremely important in paramagnetic metalloproteins. The identification, characterization, and proper structural restraining of the first coordination sphere of the metal ion(s) and its immediate neighboring regions is key to understand their biological function. The novel HSQC scheme we propose here, that we termed R2-weighted, HSQC-AP, achieves this aim by detecting signals that escaped detection in a conventional HSQC experiment and provides fully reliable R2 values in the range of 1H R2 rates ca. 50-400 s-1. Independently on the type of paramagnetic center and on the size of the molecule, this experiment decreases the radius of the blind sphere and increases the number of detectable PREs. Here, we report the validation of this approach for the case of PioC, a small protein containing a high potential 4Fe-4S cluster in the reduced [Fe4S4]2+ form. The blind sphere was contracted to a minimal extent, enabling the measurement of R2 rates for the cluster coordinating residues.
DOI: 10.1007/s10858-020-00334-w
PubMed: 32710399
PubMed Central: PMC7508935
Affiliations:
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Sacconi 6, 50019, Sesto Fiorentino, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Consorzio Interuniversitario Risonanze Magnetiche Di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Consorzio Interuniversitario Risonanze Magnetiche Di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation></author><author><name sortKey="Trindade, Ines B" sort="Trindade, Ines B" uniqKey="Trindade I" first="Inês B" last="Trindade">Inês B. 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Sacconi 6, 50019, Sesto Fiorentino, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Consorzio Interuniversitario Risonanze Magnetiche Di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Consorzio Interuniversitario Risonanze Magnetiche Di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation></author><author><name sortKey="Louro, Ricardo O" sort="Louro, Ricardo O" uniqKey="Louro R" first="Ricardo O" last="Louro">Ricardo O. Louro</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157, Oeiras, Portugal. louro@itqb.unl.pt.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157, Oeiras</wicri:regionArea><wicri:noRegion>Oeiras</wicri:noRegion></affiliation></author><author><name sortKey="Piccioli, Mario" sort="Piccioli, Mario" uniqKey="Piccioli M" first="Mario" last="Piccioli">Mario Piccioli</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. piccioli@cerm.unifi.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Consorzio Interuniversitario Risonanze Magnetiche Di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. piccioli@cerm.unifi.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Consorzio Interuniversitario Risonanze Magnetiche Di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of biomolecular NMR</title><idno type="eISSN">1573-5001</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The enhancement of nuclear relaxation rates due to the interaction with a paramagnetic center (known as Paramagnetic Relaxation Enhancement) is a powerful source of structural and dynamics information, widely used in structural biology. However, many signals affected by the hyperfine interaction relax faster than the evolution periods of common NMR experiments and therefore they are broadened beyond detection. This gives rise to a so-called blind sphere around the paramagnetic center, which is a major limitation in the use of PREs. Reducing the blind sphere is extremely important in paramagnetic metalloproteins. The identification, characterization, and proper structural restraining of the first coordination sphere of the metal ion(s) and its immediate neighboring regions is key to understand their biological function. The novel HSQC scheme we propose here, that we termed R<sub>2</sub>-weighted, HSQC-AP, achieves this aim by detecting signals that escaped detection in a conventional HSQC experiment and provides fully reliable R<sub>2</sub> values in the range of <sup>1</sup>H R<sub>2</sub> rates ca. 50-400 s<sup>-1</sup>. Independently on the type of paramagnetic center and on the size of the molecule, this experiment decreases the radius of the blind sphere and increases the number of detectable PREs. Here, we report the validation of this approach for the case of PioC, a small protein containing a high potential 4Fe-4S cluster in the reduced [Fe<sub>4</sub>S<sub>4</sub>]<sup>2+</sup> form. The blind sphere was contracted to a minimal extent, enabling the measurement of R<sub>2</sub> rates for the cluster coordinating residues.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32710399</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>06</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-5001</ISSN><JournalIssue CitedMedium="Internet"><Volume>74</Volume><Issue>8-9</Issue><PubDate><Year>2020</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of biomolecular NMR</Title><ISOAbbreviation>J Biomol NMR</ISOAbbreviation></Journal><ArticleTitle>Measuring transverse relaxation in highly paramagnetic systems.</ArticleTitle><Pagination><MedlinePgn>431-442</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s10858-020-00334-w</ELocationID><Abstract><AbstractText>The enhancement of nuclear relaxation rates due to the interaction with a paramagnetic center (known as Paramagnetic Relaxation Enhancement) is a powerful source of structural and dynamics information, widely used in structural biology. However, many signals affected by the hyperfine interaction relax faster than the evolution periods of common NMR experiments and therefore they are broadened beyond detection. This gives rise to a so-called blind sphere around the paramagnetic center, which is a major limitation in the use of PREs. Reducing the blind sphere is extremely important in paramagnetic metalloproteins. The identification, characterization, and proper structural restraining of the first coordination sphere of the metal ion(s) and its immediate neighboring regions is key to understand their biological function. The novel HSQC scheme we propose here, that we termed R<sub>2</sub>-weighted, HSQC-AP, achieves this aim by detecting signals that escaped detection in a conventional HSQC experiment and provides fully reliable R<sub>2</sub> values in the range of <sup>1</sup>H R<sub>2</sub> rates ca. 50-400 s<sup>-1</sup>. Independently on the type of paramagnetic center and on the size of the molecule, this experiment decreases the radius of the blind sphere and increases the number of detectable PREs. Here, we report the validation of this approach for the case of PioC, a small protein containing a high potential 4Fe-4S cluster in the reduced [Fe<sub>4</sub>S<sub>4</sub>]<sup>2+</sup> form. The blind sphere was contracted to a minimal extent, enabling the measurement of R<sub>2</sub> rates for the cluster coordinating residues.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Invernici</LastName><ForeName>Michele</ForeName><Initials>M</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-0312-7547</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Consorzio Interuniversitario Risonanze Magnetiche Di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Trindade</LastName><ForeName>Inês B</ForeName><Initials>IB</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-6746-8455</Identifier><AffiliationInfo><Affiliation>Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157, Oeiras, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cantini</LastName><ForeName>Francesca</ForeName><Initials>F</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-0526-6732</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Consorzio Interuniversitario Risonanze Magnetiche Di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Louro</LastName><ForeName>Ricardo O</ForeName><Initials>RO</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-2392-6450</Identifier><AffiliationInfo><Affiliation>Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157, Oeiras, Portugal. louro@itqb.unl.pt.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Piccioli</LastName><ForeName>Mario</ForeName><Initials>M</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-9882-9754</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. piccioli@cerm.unifi.it.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Consorzio Interuniversitario Risonanze Magnetiche Di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. piccioli@cerm.unifi.it.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>ISTRUCT-ERIC 4509</GrantID><Agency>Horizon 2020 Framework Programme</Agency><Country></Country></Grant><Grant><GrantID>TWINNING TIMB3 810856</GrantID><Agency>H2020 Spreading Excellence and Widening Participation</Agency><Country></Country></Grant><Grant><GrantID>CA-15133</GrantID><Agency>European Cooperation in Science and Technology</Agency><Country></Country></Grant><Grant><GrantID>2016 0985</GrantID><Agency>Ente Cassa di Risparmio di Firenze</Agency><Country></Country></Grant><Grant><GrantID>LISBOA-01-0145-FEDER-007660</GrantID><Agency>Fundação para a Ciência e a Tecnologia</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>07</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Biomol NMR</MedlineTA><NlmUniqueID>9110829</NlmUniqueID><ISSNLinking>0925-2738</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Iron sulfur proteins</Keyword><Keyword MajorTopicYN="N">NMR based structural restraints</Keyword><Keyword MajorTopicYN="N">Paramagnetic NMR</Keyword><Keyword MajorTopicYN="N">Paramagnetic relaxation enhancement</Keyword><Keyword MajorTopicYN="N">Pulse sequences</Keyword><Keyword MajorTopicYN="N">Transverse relaxation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>05</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>07</Month><Day>09</Day></PubMedPubDate><PubMedPubDate 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Feb;184(2):185-95</Citation><ArticleIdList><ArticleId IdType="pubmed">17084097</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Italie</li><li>Portugal</li></country></list><tree><country name="Italie"><noRegion><name sortKey="Invernici, Michele" sort="Invernici, Michele" uniqKey="Invernici M" first="Michele" last="Invernici">Michele Invernici</name></noRegion><name sortKey="Cantini, Francesca" sort="Cantini, Francesca" uniqKey="Cantini F" first="Francesca" last="Cantini">Francesca Cantini</name><name sortKey="Cantini, Francesca" sort="Cantini, Francesca" uniqKey="Cantini F" first="Francesca" last="Cantini">Francesca Cantini</name><name sortKey="Invernici, Michele" sort="Invernici, Michele" uniqKey="Invernici M" first="Michele" last="Invernici">Michele Invernici</name><name sortKey="Piccioli, Mario" sort="Piccioli, Mario" uniqKey="Piccioli M" first="Mario" last="Piccioli">Mario Piccioli</name><name sortKey="Piccioli, Mario" sort="Piccioli, Mario" uniqKey="Piccioli M" first="Mario" last="Piccioli">Mario Piccioli</name></country><country name="Portugal"><noRegion><name sortKey="Trindade, Ines B" sort="Trindade, Ines B" uniqKey="Trindade I" first="Inês B" last="Trindade">Inês B. Trindade</name></noRegion><name sortKey="Louro, Ricardo O" sort="Louro, Ricardo O" uniqKey="Louro R" first="Ricardo O" last="Louro">Ricardo O. Louro</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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