Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange.
Identifieur interne : 000936 ( Main/Exploration ); précédent : 000935; suivant : 000937Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange.
Auteurs : Wenbin Qi [États-Unis] ; J A CowanSource :
- Chemical communications (Cambridge, England) [ 1364-548X ] ; 2011.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Glutaredoxins, Glutathione Disulfide, Iron, Iron-Sulfur Proteins, Sulfur.
- Binding Sites, Calorimetry, Differential Scanning, Humans, Kinetics, Thermodynamics.
Abstract
Exchange of [2Fe-2S] centers between Grx2 and the cluster scaffold protein ISU, and characterization of two mutually exclusive Grx2 binding sites on ISU by isothermal titration calorimetry supports a direct link for Grx and glutathione involvement in ISU promoted Fe-S cluster biosynthesis.
DOI: 10.1039/c0cc05079b
PubMed: 21437321
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<author><name sortKey="Qi, Wenbin" sort="Qi, Wenbin" uniqKey="Qi W" first="Wenbin" last="Qi">Wenbin Qi</name>
<affiliation wicri:level="2"><nlm:affiliation>Ohio State Biochemistry Program, The Ohio State University, 100 West 18thAvenue, Columbus, OH 43210, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Ohio State Biochemistry Program, The Ohio State University, 100 West 18thAvenue, Columbus, OH 43210</wicri:regionArea>
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<author><name sortKey="Cowan, J A" sort="Cowan, J A" uniqKey="Cowan J" first="J A" last="Cowan">J A Cowan</name>
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<affiliation wicri:level="2"><nlm:affiliation>Ohio State Biochemistry Program, The Ohio State University, 100 West 18thAvenue, Columbus, OH 43210, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
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<placeName><region type="state">Ohio</region>
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<author><name sortKey="Cowan, J A" sort="Cowan, J A" uniqKey="Cowan J" first="J A" last="Cowan">J A Cowan</name>
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<series><title level="j">Chemical communications (Cambridge, England)</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term>
<term>Calorimetry, Differential Scanning (MeSH)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione Disulfide (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Iron (metabolism)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Sulfur (metabolism)</term>
<term>Thermodynamics (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Calorimétrie différentielle à balayage (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Disulfure de glutathion (métabolisme)</term>
<term>Fer (métabolisme)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Sites de fixation (MeSH)</term>
<term>Soufre (métabolisme)</term>
<term>Thermodynamique (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Glutathione Disulfide</term>
<term>Iron</term>
<term>Iron-Sulfur Proteins</term>
<term>Sulfur</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfure de glutathion</term>
<term>Fer</term>
<term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Soufre</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Calorimetry, Differential Scanning</term>
<term>Humans</term>
<term>Kinetics</term>
<term>Thermodynamics</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Calorimétrie différentielle à balayage</term>
<term>Cinétique</term>
<term>Humains</term>
<term>Sites de fixation</term>
<term>Thermodynamique</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Exchange of [2Fe-2S] centers between Grx2 and the cluster scaffold protein ISU, and characterization of two mutually exclusive Grx2 binding sites on ISU by isothermal titration calorimetry supports a direct link for Grx and glutathione involvement in ISU promoted Fe-S cluster biosynthesis.</div>
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<Month>08</Month>
<Day>09</Day>
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<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
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<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1364-548X</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>47</Volume>
<Issue>17</Issue>
<PubDate><Year>2011</Year>
<Month>May</Month>
<Day>07</Day>
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<Title>Chemical communications (Cambridge, England)</Title>
<ISOAbbreviation>Chem Commun (Camb)</ISOAbbreviation>
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<ArticleTitle>Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange.</ArticleTitle>
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<Abstract><AbstractText>Exchange of [2Fe-2S] centers between Grx2 and the cluster scaffold protein ISU, and characterization of two mutually exclusive Grx2 binding sites on ISU by isothermal titration calorimetry supports a direct link for Grx and glutathione involvement in ISU promoted Fe-S cluster biosynthesis.</AbstractText>
<CopyrightInformation>© The Royal Society of Chemistry 2011</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Qi</LastName>
<ForeName>Wenbin</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Ohio State Biochemistry Program, The Ohio State University, 100 West 18thAvenue, Columbus, OH 43210, USA.</Affiliation>
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<Author ValidYN="Y"><LastName>Cowan</LastName>
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<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>AI072443</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
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<NameOfSubstance UI="C516008">GLRX2 protein, human</NameOfSubstance>
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<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
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<NameOfSubstance UI="C506160">ISCU protein, human</NameOfSubstance>
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<Chemical><RegistryNumber>E1UOL152H7</RegistryNumber>
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<Chemical><RegistryNumber>ULW86O013H</RegistryNumber>
<NameOfSubstance UI="D019803">Glutathione Disulfide</NameOfSubstance>
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<MeshHeading><DescriptorName UI="D002152" MajorTopicYN="N">Calorimetry, Differential Scanning</DescriptorName>
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<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
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<MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName>
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