Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin.
Identifieur interne : 000859 ( Main/Exploration ); précédent : 000858; suivant : 000860Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin.
Auteurs : Lei Wang [République populaire de Chine] ; Bingjie Ouyang ; Yifei Li ; Yingang Feng ; Jean-Pierre Jacquot ; Nicolas Rouhier ; Bin XiaSource :
- Protein & cell [ 1674-8018 ] ; 2012.
Descripteurs français
- KwdFr :
- Dichroïsme circulaire (MeSH), Dimérisation (MeSH), Fer (composition chimique), Ferrédoxines (composition chimique), Ferrédoxines (métabolisme), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Glutathion (métabolisme), Ligands (MeSH), Soufre (composition chimique), Spectroscopie par résonance magnétique (MeSH), Thiols (composition chimique), Toluène (analogues et dérivés), Toluène (composition chimique).
- MESH :
- analogues et dérivés : Toluène.
- composition chimique : Fer, Ferrédoxines, Glutarédoxines, Soufre, Thiols, Toluène.
- métabolisme : Ferrédoxines, Glutarédoxines, Glutathion.
- Dichroïsme circulaire, Dimérisation, Ligands, Spectroscopie par résonance magnétique.
English descriptors
- KwdEn :
- Circular Dichroism (MeSH), Dimerization (MeSH), Ferredoxins (chemistry), Ferredoxins (metabolism), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Glutathione (metabolism), Iron (chemistry), Ligands (MeSH), Magnetic Resonance Spectroscopy (MeSH), Sulfhydryl Compounds (chemistry), Sulfur (chemistry), Toluene (analogs & derivatives), Toluene (chemistry).
- MESH :
- chemical , analogs & derivatives : Toluene.
- chemical , chemistry : Ferredoxins, Glutaredoxins, Iron, Sulfhydryl Compounds, Sulfur, Toluene.
- chemical , metabolism : Ferredoxins, Glutaredoxins, Glutathione.
- Circular Dichroism, Dimerization, Ligands, Magnetic Resonance Spectroscopy.
Abstract
Holo glutaredoxin (Grx) is a homo-dimer that bridges a [2Fe-2S] cluster with two glutathione (GSH) ligands. In this study, both monothiol and dithiol holo Grxs are found capable of transferring their iron-sulfur (FeS) cluster to an apo ferredoxin (Fdx) through direct interaction, regardless of FeS cluster stability in holo Grxs. The ligand GSH molecules in holo Grxs are unstable and can be exchanged with free GSH, which inhibits the FeS cluster transfer from holo Grxs to apo Fdx. This phenomenon suggests a novel role of GSH in FeS cluster trafficking.
DOI: 10.1007/s13238-012-2051-4
PubMed: 22886498
PubMed Central: PMC4875373
Affiliations:
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last="Rouhier">Nicolas Rouhier</name></author><author><name sortKey="Xia, Bin" sort="Xia, Bin" uniqKey="Xia B" first="Bin" last="Xia">Bin Xia</name></author></analytic><series><title level="j">Protein & cell</title><idno type="eISSN">1674-8018</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Circular Dichroism (MeSH)</term><term>Dimerization (MeSH)</term><term>Ferredoxins (chemistry)</term><term>Ferredoxins (metabolism)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Iron (chemistry)</term><term>Ligands (MeSH)</term><term>Magnetic Resonance Spectroscopy (MeSH)</term><term>Sulfhydryl Compounds (chemistry)</term><term>Sulfur (chemistry)</term><term>Toluene (analogs & derivatives)</term><term>Toluene (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Dichroïsme circulaire (MeSH)</term><term>Dimérisation (MeSH)</term><term>Fer (composition chimique)</term><term>Ferrédoxines (composition chimique)</term><term>Ferrédoxines (métabolisme)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Ligands (MeSH)</term><term>Soufre (composition chimique)</term><term>Spectroscopie par résonance magnétique (MeSH)</term><term>Thiols (composition chimique)</term><term>Toluène (analogues et dérivés)</term><term>Toluène (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Toluene</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ferredoxins</term><term>Glutaredoxins</term><term>Iron</term><term>Sulfhydryl Compounds</term><term>Sulfur</term><term>Toluene</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Ferredoxins</term><term>Glutaredoxins</term><term>Glutathione</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Toluène</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Fer</term><term>Ferrédoxines</term><term>Glutarédoxines</term><term>Soufre</term><term>Thiols</term><term>Toluène</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Ferrédoxines</term><term>Glutarédoxines</term><term>Glutathion</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Circular Dichroism</term><term>Dimerization</term><term>Ligands</term><term>Magnetic Resonance Spectroscopy</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dichroïsme circulaire</term><term>Dimérisation</term><term>Ligands</term><term>Spectroscopie par résonance magnétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Holo glutaredoxin (Grx) is a homo-dimer that bridges a [2Fe-2S] cluster with two glutathione (GSH) ligands. In this study, both monothiol and dithiol holo Grxs are found capable of transferring their iron-sulfur (FeS) cluster to an apo ferredoxin (Fdx) through direct interaction, regardless of FeS cluster stability in holo Grxs. The ligand GSH molecules in holo Grxs are unstable and can be exchanged with free GSH, which inhibits the FeS cluster transfer from holo Grxs to apo Fdx. This phenomenon suggests a novel role of GSH in FeS cluster trafficking.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22886498</PMID><DateCompleted><Year>2013</Year><Month>01</Month><Day>03</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1674-8018</ISSN><JournalIssue CitedMedium="Internet"><Volume>3</Volume><Issue>9</Issue><PubDate><Year>2012</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Protein & cell</Title><ISOAbbreviation>Protein Cell</ISOAbbreviation></Journal><ArticleTitle>Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin.</ArticleTitle><Pagination><MedlinePgn>714-21</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s13238-012-2051-4</ELocationID><Abstract><AbstractText>Holo glutaredoxin (Grx) is a homo-dimer that bridges a [2Fe-2S] cluster with two glutathione (GSH) ligands. In this study, both monothiol and dithiol holo Grxs are found capable of transferring their iron-sulfur (FeS) cluster to an apo ferredoxin (Fdx) through direct interaction, regardless of FeS cluster stability in holo Grxs. The ligand GSH molecules in holo Grxs are unstable and can be exchanged with free GSH, which inhibits the FeS cluster transfer from holo Grxs to apo Fdx. 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ValidYN="Y"><LastName>Xia</LastName><ForeName>Bin</ForeName><Initials>B</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><ArticleDate DateType="Electronic"><Year>2012</Year><Month>08</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Protein Cell</MedlineTA><NlmUniqueID>101532368</NlmUniqueID><ISSNLinking>1674-800X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005288">Ferredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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sort="Feng, Yingang" uniqKey="Feng Y" first="Yingang" last="Feng">Yingang Feng</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Li, Yifei" sort="Li, Yifei" uniqKey="Li Y" first="Yifei" last="Li">Yifei Li</name><name sortKey="Ouyang, Bingjie" sort="Ouyang, Bingjie" uniqKey="Ouyang B" first="Bingjie" last="Ouyang">Bingjie Ouyang</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Xia, Bin" sort="Xia, Bin" uniqKey="Xia B" first="Bin" last="Xia">Bin Xia</name></noCountry><country name="République populaire de Chine"><region name="Pékin"><name sortKey="Wang, Lei" sort="Wang, Lei" uniqKey="Wang L" first="Lei" last="Wang">Lei Wang</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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