Thiol-disulfide exchange between glutaredoxin and glutathione.
Identifieur interne : 000979 ( Main/Exploration ); précédent : 000978; suivant : 000980Thiol-disulfide exchange between glutaredoxin and glutathione.
Auteurs : Rasmus Iversen [Danemark] ; Peter Anders Andersen ; Kristine Steen Jensen ; Jakob R. Winther ; Bent W. SigurskjoldSource :
- Biochemistry [ 1520-4995 ] ; 2010.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Concentration en ions d'hydrogène (MeSH), Disulfures (composition chimique), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Glutathion (composition chimique), Glutathion (métabolisme), Pliage des protéines (MeSH), Température (MeSH), Thermodynamique (MeSH), Thiols (composition chimique).
- MESH :
- composition chimique : Disulfures, Glutarédoxines, Glutathion, Thiols.
- métabolisme : Glutarédoxines, Glutathion.
- Catalyse, Concentration en ions d'hydrogène, Pliage des protéines, Température, Thermodynamique.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Disulfides, Glutaredoxins, Glutathione, Sulfhydryl Compounds.
- chemical , metabolism : Glutaredoxins, Glutathione.
- Catalysis, Hydrogen-Ion Concentration, Protein Folding, Temperature, Thermodynamics.
Abstract
Glutaredoxins are ubiquitous thiol-disulfide oxidoreductases which catalyze the reduction of glutathione-protein mixed disulfides. Belonging to the thioredoxin family, they contain a conserved active site CXXC motif. The N-proximal active site cysteine can form a mixed disulfide with glutathione or an intramolecular disulfide with the C-proximal cysteine. The C-proximal cysteine is not known to be involved in the catalytic mechanism. The stability of the mixed disulfide with glutathione has been investigated in detail using a mutant variant of yeast glutaredoxin 1, in which the C-proximal active site cysteine has been replaced with serine. The exchange reaction between the reduced protein and oxidized glutathione leading to formation of the mixed disulfide could readily be monitored by isothermal titration calorimetry (ITC) due to the enthalpic contributions from the noncovalent interactions and the protonation of glutathione thiolate. An algorithm for the analysis of this type of reaction by ITC was developed and showed that the interaction is enthalpy driven with a large entropy penalty. The applicability of the method was verified by a mass spectrometry-based approach, which gave a standard reduction potential of -295 mV for the mixed disulfide. In another set of experiments, the pK(a) value of the active site cysteine was determined. In line with what has been observed for other glutaredoxins, this cysteine was found to have a very low pK(a) value. The glutathionylation of glutaredoxin was shown to have a substantial effect on the thermal stability of the protein as revealed by differential scanning calorimetry.
DOI: 10.1021/bi9015956
PubMed: 19968277
Affiliations:
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Le document en format XML
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Winther</name></author><author><name sortKey="Sigurskjold, Bent W" sort="Sigurskjold, Bent W" uniqKey="Sigurskjold B" first="Bent W" last="Sigurskjold">Bent W. Sigurskjold</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:19968277</idno><idno type="pmid">19968277</idno><idno type="doi">10.1021/bi9015956</idno><idno type="wicri:Area/Main/Corpus">000A52</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000A52</idno><idno type="wicri:Area/Main/Curation">000A52</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000A52</idno><idno type="wicri:Area/Main/Exploration">000A52</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Thiol-disulfide exchange between glutaredoxin and glutathione.</title><author><name sortKey="Iversen, Rasmus" sort="Iversen, Rasmus" uniqKey="Iversen R" first="Rasmus" last="Iversen">Rasmus Iversen</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biology, University of Copenhagen, Copenhagen Biocenter, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark.</nlm:affiliation><country xml:lang="fr">Danemark</country><wicri:regionArea>Department of Biology, University of Copenhagen, Copenhagen Biocenter, Ole Maaløes Vej 5, DK-2200 Copenhagen N</wicri:regionArea><wicri:noRegion>DK-2200 Copenhagen N</wicri:noRegion></affiliation></author><author><name sortKey="Andersen, Peter Anders" sort="Andersen, Peter Anders" uniqKey="Andersen P" first="Peter Anders" last="Andersen">Peter Anders Andersen</name></author><author><name sortKey="Jensen, Kristine Steen" sort="Jensen, Kristine Steen" uniqKey="Jensen K" first="Kristine Steen" last="Jensen">Kristine Steen Jensen</name></author><author><name sortKey="Winther, Jakob R" sort="Winther, Jakob R" uniqKey="Winther J" first="Jakob R" last="Winther">Jakob R. Winther</name></author><author><name sortKey="Sigurskjold, Bent W" sort="Sigurskjold, Bent W" uniqKey="Sigurskjold B" first="Bent W" last="Sigurskjold">Bent W. Sigurskjold</name></author></analytic><series><title level="j">Biochemistry</title><idno type="eISSN">1520-4995</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Catalysis (MeSH)</term><term>Disulfides (chemistry)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (chemistry)</term><term>Glutathione (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Protein Folding (MeSH)</term><term>Sulfhydryl Compounds (chemistry)</term><term>Temperature (MeSH)</term><term>Thermodynamics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Disulfures (composition chimique)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (composition chimique)</term><term>Glutathion (métabolisme)</term><term>Pliage des protéines (MeSH)</term><term>Température (MeSH)</term><term>Thermodynamique (MeSH)</term><term>Thiols (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term><term>Glutaredoxins</term><term>Glutathione</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Glutathione</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Disulfures</term><term>Glutarédoxines</term><term>Glutathion</term><term>Thiols</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Glutathion</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Hydrogen-Ion Concentration</term><term>Protein Folding</term><term>Temperature</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Concentration en ions d'hydrogène</term><term>Pliage des protéines</term><term>Température</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins are ubiquitous thiol-disulfide oxidoreductases which catalyze the reduction of glutathione-protein mixed disulfides. Belonging to the thioredoxin family, they contain a conserved active site CXXC motif. The N-proximal active site cysteine can form a mixed disulfide with glutathione or an intramolecular disulfide with the C-proximal cysteine. The C-proximal cysteine is not known to be involved in the catalytic mechanism. The stability of the mixed disulfide with glutathione has been investigated in detail using a mutant variant of yeast glutaredoxin 1, in which the C-proximal active site cysteine has been replaced with serine. The exchange reaction between the reduced protein and oxidized glutathione leading to formation of the mixed disulfide could readily be monitored by isothermal titration calorimetry (ITC) due to the enthalpic contributions from the noncovalent interactions and the protonation of glutathione thiolate. An algorithm for the analysis of this type of reaction by ITC was developed and showed that the interaction is enthalpy driven with a large entropy penalty. The applicability of the method was verified by a mass spectrometry-based approach, which gave a standard reduction potential of -295 mV for the mixed disulfide. In another set of experiments, the pK(a) value of the active site cysteine was determined. In line with what has been observed for other glutaredoxins, this cysteine was found to have a very low pK(a) value. The glutathionylation of glutaredoxin was shown to have a substantial effect on the thermal stability of the protein as revealed by differential scanning calorimetry.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19968277</PMID><DateCompleted><Year>2010</Year><Month>03</Month><Day>19</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>49</Volume><Issue>4</Issue><PubDate><Year>2010</Year><Month>Feb</Month><Day>02</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Thiol-disulfide exchange between glutaredoxin and glutathione.</ArticleTitle><Pagination><MedlinePgn>810-20</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/bi9015956</ELocationID><Abstract><AbstractText>Glutaredoxins are ubiquitous thiol-disulfide oxidoreductases which catalyze the reduction of glutathione-protein mixed disulfides. Belonging to the thioredoxin family, they contain a conserved active site CXXC motif. The N-proximal active site cysteine can form a mixed disulfide with glutathione or an intramolecular disulfide with the C-proximal cysteine. The C-proximal cysteine is not known to be involved in the catalytic mechanism. The stability of the mixed disulfide with glutathione has been investigated in detail using a mutant variant of yeast glutaredoxin 1, in which the C-proximal active site cysteine has been replaced with serine. The exchange reaction between the reduced protein and oxidized glutathione leading to formation of the mixed disulfide could readily be monitored by isothermal titration calorimetry (ITC) due to the enthalpic contributions from the noncovalent interactions and the protonation of glutathione thiolate. An algorithm for the analysis of this type of reaction by ITC was developed and showed that the interaction is enthalpy driven with a large entropy penalty. The applicability of the method was verified by a mass spectrometry-based approach, which gave a standard reduction potential of -295 mV for the mixed disulfide. In another set of experiments, the pK(a) value of the active site cysteine was determined. In line with what has been observed for other glutaredoxins, this cysteine was found to have a very low pK(a) value. The glutathionylation of glutaredoxin was shown to have a substantial effect on the thermal stability of the protein as revealed by differential scanning calorimetry.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Iversen</LastName><ForeName>Rasmus</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Copenhagen, Copenhagen Biocenter, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Andersen</LastName><ForeName>Peter Anders</ForeName><Initials>PA</Initials></Author><Author ValidYN="Y"><LastName>Jensen</LastName><ForeName>Kristine Steen</ForeName><Initials>KS</Initials></Author><Author ValidYN="Y"><LastName>Winther</LastName><ForeName>Jakob R</ForeName><Initials>JR</Initials></Author><Author ValidYN="Y"><LastName>Sigurskjold</LastName><ForeName>Bent W</ForeName><Initials>BW</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>12</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>12</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>3</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19968277</ArticleId><ArticleId IdType="doi">10.1021/bi9015956</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Danemark</li></country></list><tree><noCountry><name sortKey="Andersen, Peter Anders" sort="Andersen, Peter Anders" uniqKey="Andersen P" first="Peter Anders" last="Andersen">Peter Anders Andersen</name><name sortKey="Jensen, Kristine Steen" sort="Jensen, Kristine Steen" uniqKey="Jensen K" first="Kristine Steen" last="Jensen">Kristine Steen Jensen</name><name sortKey="Sigurskjold, Bent W" sort="Sigurskjold, Bent W" uniqKey="Sigurskjold B" first="Bent W" last="Sigurskjold">Bent W. Sigurskjold</name><name sortKey="Winther, Jakob R" sort="Winther, Jakob R" uniqKey="Winther J" first="Jakob R" last="Winther">Jakob R. Winther</name></noCountry><country name="Danemark"><noRegion><name sortKey="Iversen, Rasmus" sort="Iversen, Rasmus" uniqKey="Iversen R" first="Rasmus" last="Iversen">Rasmus Iversen</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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