Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction.
Identifieur interne : 001093 ( Main/Exploration ); précédent : 001092; suivant : 001094Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction.
Auteurs : J. Shi [États-Unis] ; A. Vlamis-Gardikas ; F. Aslund ; A. Holmgren ; B P RosenSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1999.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Arsenates, Arsenites, Bacterial Proteins, Hydrogen, Proteins.
- metabolism : Escherichia coli.
- Electron Transport, Glutaredoxins, Oxidoreductases.
Abstract
In Escherichia coli ArsC catalyzes the reduction of arsenate to arsenite using GSH with glutaredoxin as electron donors. E. coli has three glutaredoxins: 1, 2, and 3, each with a classical -Cys-Pro-Tyr-Cys- active site. Glutaredoxin 2 is the major glutathione disulfide oxidoreductase in E. coli, but its function remains unknown. In this report glutaredoxin 2 is shown to be the most effective hydrogen donor for the reduction of arsenate by ArsC. Analysis of single or double cysteine-to-serine substitutions in the active site of the three glutaredoxins indicated that only the N-terminal cysteine residue is essential for activity. This suggests that, during the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.
DOI: 10.1074/jbc.274.51.36039
PubMed: 10593884
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction.</title><author><name sortKey="Shi, J" sort="Shi, J" uniqKey="Shi J" first="J" last="Shi">J. Shi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201</wicri:regionArea><wicri:noRegion>Michigan 48201</wicri:noRegion></affiliation></author><author><name sortKey="Vlamis Gardikas, A" sort="Vlamis Gardikas, A" uniqKey="Vlamis Gardikas A" first="A" last="Vlamis-Gardikas">A. Vlamis-Gardikas</name></author><author><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author><author><name sortKey="Rosen, B P" sort="Rosen, B P" uniqKey="Rosen B" first="B P" last="Rosen">B P Rosen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10593884</idno><idno type="pmid">10593884</idno><idno type="doi">10.1074/jbc.274.51.36039</idno><idno type="wicri:Area/Main/Corpus">001089</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001089</idno><idno type="wicri:Area/Main/Curation">001089</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001089</idno><idno type="wicri:Area/Main/Exploration">001089</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction.</title><author><name sortKey="Shi, J" sort="Shi, J" uniqKey="Shi J" first="J" last="Shi">J. Shi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201</wicri:regionArea><wicri:noRegion>Michigan 48201</wicri:noRegion></affiliation></author><author><name sortKey="Vlamis Gardikas, A" sort="Vlamis Gardikas, A" uniqKey="Vlamis Gardikas A" first="A" last="Vlamis-Gardikas">A. Vlamis-Gardikas</name></author><author><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author><author><name sortKey="Rosen, B P" sort="Rosen, B P" uniqKey="Rosen B" first="B P" last="Rosen">B P Rosen</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arsenates (metabolism)</term><term>Arsenites (metabolism)</term><term>Bacterial Proteins (metabolism)</term><term>Electron Transport (MeSH)</term><term>Escherichia coli (metabolism)</term><term>Glutaredoxins (MeSH)</term><term>Hydrogen (metabolism)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arséniates (métabolisme)</term><term>Arsénites (métabolisme)</term><term>Escherichia coli (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Hydrogène (métabolisme)</term><term>Oxidoreductases (MeSH)</term><term>Protéines (métabolisme)</term><term>Protéines bactériennes (métabolisme)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arsenates</term><term>Arsenites</term><term>Bacterial Proteins</term><term>Hydrogen</term><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arséniates</term><term>Arsénites</term><term>Escherichia coli</term><term>Hydrogène</term><term>Protéines</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Transport</term><term>Glutaredoxins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In Escherichia coli ArsC catalyzes the reduction of arsenate to arsenite using GSH with glutaredoxin as electron donors. E. coli has three glutaredoxins: 1, 2, and 3, each with a classical -Cys-Pro-Tyr-Cys- active site. Glutaredoxin 2 is the major glutathione disulfide oxidoreductase in E. coli, but its function remains unknown. In this report glutaredoxin 2 is shown to be the most effective hydrogen donor for the reduction of arsenate by ArsC. Analysis of single or double cysteine-to-serine substitutions in the active site of the three glutaredoxins indicated that only the N-terminal cysteine residue is essential for activity. This suggests that, during the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10593884</PMID><DateCompleted><Year>2000</Year><Month>01</Month><Day>27</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>274</Volume><Issue>51</Issue><PubDate><Year>1999</Year><Month>Dec</Month><Day>17</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction.</ArticleTitle><Pagination><MedlinePgn>36039-42</MedlinePgn></Pagination><Abstract><AbstractText>In Escherichia coli ArsC catalyzes the reduction of arsenate to arsenite using GSH with glutaredoxin as electron donors. E. coli has three glutaredoxins: 1, 2, and 3, each with a classical -Cys-Pro-Tyr-Cys- active site. Glutaredoxin 2 is the major glutathione disulfide oxidoreductase in E. coli, but its function remains unknown. In this report glutaredoxin 2 is shown to be the most effective hydrogen donor for the reduction of arsenate by ArsC. Analysis of single or double cysteine-to-serine substitutions in the active site of the three glutaredoxins indicated that only the N-terminal cysteine residue is essential for activity. This suggests that, during the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shi</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vlamis-Gardikas</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Aslund</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Rosen</LastName><ForeName>B P</ForeName><Initials>BP</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM52216</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001149">Arsenates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018053">Arsenites</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>7YNJ3PO35Z</RegistryNumber><NameOfSubstance UI="D006859">Hydrogen</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>N5509X556J</RegistryNumber><NameOfSubstance UI="C015001">arsenite</NameOfSubstance></Chemical><Chemical><RegistryNumber>N7CIZ75ZPN</RegistryNumber><NameOfSubstance UI="C025657">arsenic acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001149" MajorTopicYN="N">Arsenates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018053" MajorTopicYN="N">Arsenites</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006859" MajorTopicYN="N">Hydrogen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>12</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>12</Month><Day>14</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>12</Month><Day>14</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10593884</ArticleId><ArticleId IdType="doi">10.1074/jbc.274.51.36039</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Rosen, B P" sort="Rosen, B P" uniqKey="Rosen B" first="B P" last="Rosen">B P Rosen</name><name sortKey="Vlamis Gardikas, A" sort="Vlamis Gardikas, A" uniqKey="Vlamis Gardikas A" first="A" last="Vlamis-Gardikas">A. Vlamis-Gardikas</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Shi, J" sort="Shi, J" uniqKey="Shi J" first="J" last="Shi">J. Shi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001093 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001093 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:10593884
|texte= Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:10593884" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |