1H, 13C and 15N assignment of the paramagnetic high potential iron-sulfur protein (HiPIP) PioC from Rhodopseudomonas palustris TIE-1.
Identifieur interne : 000188 ( Main/Exploration ); précédent : 000187; suivant : 0001891H, 13C and 15N assignment of the paramagnetic high potential iron-sulfur protein (HiPIP) PioC from Rhodopseudomonas palustris TIE-1.
Auteurs : Inês B. Trindade [Portugal] ; Michele Invernici [Italie] ; Francesca Cantini [Italie] ; Ricardo O. Louro [Portugal] ; Mario Piccioli [Italie]Source :
- Biomolecular NMR assignments [ 1874-270X ] ; 2020.
Abstract
High potential iron-sulfur proteins (HiPIPs) are a class of small proteins (50-100 aa residues), containing a 4Fe-4S iron-sulfur cluster. The 4Fe-4S cluster shuttles between the oxidation states [Fe4S4]3+/2+, with a positive redox potential in the range (500-50 mV) throughout the different known HiPIPs. Both oxidation states are paramagnetic at room temperature. HiPIPs are electron transfer proteins, isolated from photosynthetic bacteria and usually provide electrons to the photosynthetic reaction-center. PioC, the HIPIP isolated from Rhodopseudomonas palustris TIE-1, is the smallest among all known HiPIPs. Despite their small dimensions, an extensive NMR assignment is only available for two of them, because paramagnetism prevents the straightforward assignment of all resonances. We report here the complete NMR assignment of 1H, 13C and 15N signals for the reduced [Fe4S4]2+ state of the protein. A set of double and triple resonance experiments performed with standardized parameters/datasets provided the assignment of about 72% of the residues. The almost complete resonance assignment (99.5% of backbone and ca. 90% of side chain resonances) was achieved by combining the above information with those obtained using a second set of NMR experiments, in which acquisition and processing parameters, as well as pulse sequences design, were optimized to account for the peculiar features of this paramagnetic protein.
DOI: 10.1007/s12104-020-09947-6
PubMed: 32415427
PubMed Central: PMC7462912
Affiliations:
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Trindade</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.</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="Invernici, Michele" sort="Invernici, Michele" uniqKey="Invernici M" first="Michele" last="Invernici">Michele Invernici</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center (CERM), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation></author><author><name sortKey="Cantini, Francesca" sort="Cantini, Francesca" uniqKey="Cantini F" first="Francesca" last="Cantini">Francesca Cantini</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center (CERM), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, 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), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), 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), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biomolecular NMR assignments</title><idno type="eISSN">1874-270X</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">High potential iron-sulfur proteins (HiPIPs) are a class of small proteins (50-100 aa residues), containing a 4Fe-4S iron-sulfur cluster. The 4Fe-4S cluster shuttles between the oxidation states [Fe<sub>4</sub>S<sub>4</sub>]<sup>3+/2+</sup>, with a positive redox potential in the range (500-50 mV) throughout the different known HiPIPs. Both oxidation states are paramagnetic at room temperature. HiPIPs are electron transfer proteins, isolated from photosynthetic bacteria and usually provide electrons to the photosynthetic reaction-center. PioC, the HIPIP isolated from Rhodopseudomonas palustris TIE-1, is the smallest among all known HiPIPs. Despite their small dimensions, an extensive NMR assignment is only available for two of them, because paramagnetism prevents the straightforward assignment of all resonances. We report here the complete NMR assignment of <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N signals for the reduced [Fe<sub>4</sub>S<sub>4</sub>]<sup>2+</sup> state of the protein. A set of double and triple resonance experiments performed with standardized parameters/datasets provided the assignment of about 72% of the residues. The almost complete resonance assignment (99.5% of backbone and ca. 90% of side chain resonances) was achieved by combining the above information with those obtained using a second set of NMR experiments, in which acquisition and processing parameters, as well as pulse sequences design, were optimized to account for the peculiar features of this paramagnetic protein.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32415427</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1874-270X</ISSN><JournalIssue CitedMedium="Internet"><Volume>14</Volume><Issue>2</Issue><PubDate><Year>2020</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Biomolecular NMR assignments</Title><ISOAbbreviation>Biomol NMR Assign</ISOAbbreviation></Journal><ArticleTitle><sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N assignment of the paramagnetic high potential iron-sulfur protein (HiPIP) PioC from Rhodopseudomonas palustris TIE-1.</ArticleTitle><Pagination><MedlinePgn>211-215</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s12104-020-09947-6</ELocationID><Abstract><AbstractText>High potential iron-sulfur proteins (HiPIPs) are a class of small proteins (50-100 aa residues), containing a 4Fe-4S iron-sulfur cluster. The 4Fe-4S cluster shuttles between the oxidation states [Fe<sub>4</sub>S<sub>4</sub>]<sup>3+/2+</sup>, with a positive redox potential in the range (500-50 mV) throughout the different known HiPIPs. Both oxidation states are paramagnetic at room temperature. HiPIPs are electron transfer proteins, isolated from photosynthetic bacteria and usually provide electrons to the photosynthetic reaction-center. PioC, the HIPIP isolated from Rhodopseudomonas palustris TIE-1, is the smallest among all known HiPIPs. Despite their small dimensions, an extensive NMR assignment is only available for two of them, because paramagnetism prevents the straightforward assignment of all resonances. We report here the complete NMR assignment of <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N signals for the reduced [Fe<sub>4</sub>S<sub>4</sub>]<sup>2+</sup> state of the protein. A set of double and triple resonance experiments performed with standardized parameters/datasets provided the assignment of about 72% of the residues. The almost complete resonance assignment (99.5% of backbone and ca. 90% of side chain resonances) was achieved by combining the above information with those obtained using a second set of NMR experiments, in which acquisition and processing parameters, as well as pulse sequences design, were optimized to account for the peculiar features of this paramagnetic protein.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Trindade</LastName><ForeName>Inês B</ForeName><Initials>IB</Initials><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>Invernici</LastName><ForeName>Michele</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center (CERM), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cantini</LastName><ForeName>Francesca</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center (CERM), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Louro</LastName><ForeName>Ricardo O</ForeName><Initials>RO</Initials><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), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. piccioli@cerm.unifi.it.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>CA15133</GrantID><Agency>European Cooperation in Science and Technology</Agency><Country></Country></Grant><Grant><GrantID>TIMB3-Project 810856</GrantID><Agency>Horizon 2020 ()</Agency><Country></Country></Grant><Grant><GrantID>PID 4509</GrantID><Agency>INSTRUCT-ERIC</Agency><Country></Country></Grant><Grant><GrantID>2016-0985</GrantID><Agency>Ente Cassa di Risparmio di Firenze</Agency><Country></Country></Grant><Grant><GrantID>PD/BD/135187/2017</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>05</Month><Day>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biomol NMR Assign</MedlineTA><NlmUniqueID>101472371</NlmUniqueID><ISSNLinking>1874-270X</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Fast nuclear relaxation</Keyword><Keyword MajorTopicYN="N">High potential iron–sulfur proteins</Keyword><Keyword MajorTopicYN="N">Metalloproteins</Keyword><Keyword MajorTopicYN="N">Paramagnetic NMR</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>03</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>05</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>5</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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