How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?
Identifieur interne : 000C81 ( Main/Exploration ); précédent : 000C80; suivant : 000C82How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?
Auteurs : Carsten Berndt [Suède] ; Christoph Hudemann ; Eva-Maria Hanschmann ; Rebecca Axelsson ; Arne Holmgren ; Christopher Horst LilligSource :
- Antioxidants & redox signaling [ 1523-0864 ] ; 2007.
Descripteurs français
- KwdFr :
- Ferrosulfoprotéines (génétique), Ferrosulfoprotéines (métabolisme), Glutarédoxines (MeSH), Glutathion (métabolisme), Humains (MeSH), Mitochondries (métabolisme), Modèles biologiques (MeSH), Mutagenèse dirigée (MeSH), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Régulation de l'expression des gènes (MeSH).
- MESH :
- génétique : Ferrosulfoprotéines, Oxidoreductases.
- métabolisme : Ferrosulfoprotéines, Glutathion, Mitochondries, Oxidoreductases.
- Glutarédoxines, Humains, Modèles biologiques, Mutagenèse dirigée, Régulation de l'expression des gènes.
English descriptors
- KwdEn :
- Gene Expression Regulation (MeSH), Glutaredoxins (MeSH), Glutathione (metabolism), Humans (MeSH), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Mitochondria (metabolism), Models, Biological (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidoreductases (genetics), Oxidoreductases (metabolism).
- MESH :
- chemical , genetics : Iron-Sulfur Proteins, Oxidoreductases.
- chemical , metabolism : Glutathione, Iron-Sulfur Proteins, Oxidoreductases.
- chemical : Glutaredoxins.
- metabolism : Mitochondria.
- Gene Expression Regulation, Humans, Models, Biological, Mutagenesis, Site-Directed.
Abstract
Human mitochondrial glutaredoxin (Grx2) was described as the first iron-sulfur protein from the thioredoxin superfamily of proteins. The [2Fe-2S] cluster was proposed to serve as redox sensor for the activation of Grx2 during oxidative stress. The authors have demonstrated that the iron-sulfur cluster is complexed by the two N-terminal active site thiols of two Grx2 monomers and two molecules of glutathione that are bound noncovalently to the proteins and in equilibrium with glutathione in solution. When reduced glutathione becomes the limiting factor for cluster coordination, the holo-Grx2 complex dissociates, yielding enzymatically active Grx2.
DOI: 10.1089/ars.2007.9.151
PubMed: 17115894
Affiliations:
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Le document en format XML
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sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name></author><author><name sortKey="Axelsson, Rebecca" sort="Axelsson, Rebecca" uniqKey="Axelsson R" first="Rebecca" last="Axelsson">Rebecca Axelsson</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author><author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17115894</idno><idno type="pmid">17115894</idno><idno type="doi">10.1089/ars.2007.9.151</idno><idno type="wicri:Area/Main/Corpus">000C94</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" 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Regulation</term><term>Humans</term><term>Models, Biological</term><term>Mutagenesis, Site-Directed</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Glutarédoxines</term><term>Humains</term><term>Modèles biologiques</term><term>Mutagenèse dirigée</term><term>Régulation de l'expression des gènes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Human mitochondrial glutaredoxin (Grx2) was described as the first iron-sulfur protein from the thioredoxin superfamily of proteins. The [2Fe-2S] cluster was proposed to serve as redox sensor for the activation of Grx2 during oxidative stress. The authors have demonstrated that the iron-sulfur cluster is complexed by the two N-terminal active site thiols of two Grx2 monomers and two molecules of glutathione that are bound noncovalently to the proteins and in equilibrium with glutathione in solution. When reduced glutathione becomes the limiting factor for cluster coordination, the holo-Grx2 complex dissociates, yielding enzymatically active Grx2.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17115894</PMID><DateCompleted><Year>2007</Year><Month>04</Month><Day>25</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1523-0864</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>1</Issue><PubDate><Year>2007</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?</ArticleTitle><Pagination><MedlinePgn>151-7</MedlinePgn></Pagination><Abstract><AbstractText>Human mitochondrial glutaredoxin (Grx2) was described as the first iron-sulfur protein from the thioredoxin superfamily of proteins. The [2Fe-2S] cluster was proposed to serve as redox sensor for the activation of Grx2 during oxidative stress. The authors have demonstrated that the iron-sulfur cluster is complexed by the two N-terminal active site thiols of two Grx2 monomers and two molecules of glutathione that are bound noncovalently to the proteins and in equilibrium with glutathione in solution. 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last="Holmgren">Arne Holmgren</name><name sortKey="Hudemann, Christoph" sort="Hudemann, Christoph" uniqKey="Hudemann C" first="Christoph" last="Hudemann">Christoph Hudemann</name><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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