In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?
Identifieur interne : 000751 ( Main/Exploration ); précédent : 000750; suivant : 000752In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?
Auteurs : Jérémy Couturier [France] ; Pascalita Prosper ; Alison M. Winger ; Arnaud Hecker ; Masakazu Hirasawa ; David B. Knaff ; Pierre Gans ; Jean-Pierre Jacquot ; Alda Navaza ; Ahmed Haouz ; Nicolas RouhierSource :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2013.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Conformation des protéines (MeSH), Motifs et domaines d'intéraction protéique (MeSH), Multimérisation de protéines (MeSH), Myeloperoxidase (métabolisme), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Peroxirédoxines (composition chimique), Peroxirédoxines (métabolisme), Réducteurs (métabolisme), Thermotoga maritima (métabolisme), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Peroxirédoxines.
- métabolisme : Myeloperoxidase, Oxidoreductases, Peroxirédoxines, Réducteurs, Thermotoga maritima, Thiorédoxines.
- Catalyse, Conformation des protéines, Motifs et domaines d'intéraction protéique, Multimérisation de protéines, Oxydoréduction.
English descriptors
- KwdEn :
- Catalysis (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (metabolism), Peroxidase (metabolism), Peroxiredoxins (chemistry), Peroxiredoxins (metabolism), Protein Conformation (MeSH), Protein Interaction Domains and Motifs (MeSH), Protein Multimerization (MeSH), Reducing Agents (metabolism), Thermotoga maritima (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , chemistry : Peroxiredoxins.
- chemical , metabolism : Oxidoreductases, Peroxidase, Peroxiredoxins, Reducing Agents, Thioredoxins.
- metabolism : Thermotoga maritima.
- Catalysis, Oxidation-Reduction, Protein Conformation, Protein Interaction Domains and Motifs, Protein Multimerization.
Abstract
Three peroxiredoxins (Prxs) were identified in Thermotoga maritima, which possesses neither glutathione nor typical thioredoxins: one of the Prx6 class; one 2-Cys PrxBCP; and a unique hybrid protein containing an N-terminal 1-Cys PrxBCP domain fused to a flavin mononucleotide-containing nitroreductase (Ntr) domain. No peroxidase activity was detected for Prx6, whereas both bacterioferritin comigratory proteins (BCPs) were regenerated by a NADH/thioredoxin reductase/glutaredoxin (Grx)-like system, constituting a unique peroxide removal system. Only two of the three Grx-like proteins were able to support peroxidase activity. The inability of TmGrx1 to regenerate oxidized 2-Cys PrxBCP probably results from the thermodynamically unfavorable difference in their disulfide/dithiol E(m) values, -150 and -315 mV, respectively. Mutagenesis of the Prx-Ntr fusion, combined with kinetic and structural analyses, indicated that electrons are not transferred between its two domains. However, their separate activities could function in a complementary manner, with peroxide originating from the chromate reductase activity of the Ntr domain reduced by the Prx domain.
DOI: 10.1089/ars.2012.4739
PubMed: 22866991
PubMed Central: PMC3613187
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?</title><author><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><affiliation wicri:level="1"><nlm:affiliation>Unité Mixte de Recherches 1136 INRA-Lorraine Université, Interactions Arbres-Microorganismes, IFR 110, Faculté des Sciences, Vandoeuvre Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Unité Mixte de Recherches 1136 INRA-Lorraine Université, Interactions Arbres-Microorganismes, IFR 110, Faculté des Sciences, Vandoeuvre Cedex</wicri:regionArea><wicri:noRegion>Vandoeuvre Cedex</wicri:noRegion><wicri:noRegion>Vandoeuvre Cedex</wicri:noRegion></affiliation></author><author><name sortKey="Prosper, Pascalita" sort="Prosper, Pascalita" uniqKey="Prosper P" first="Pascalita" last="Prosper">Pascalita Prosper</name></author><author><name sortKey="Winger, Alison M" sort="Winger, Alison M" uniqKey="Winger A" first="Alison M" last="Winger">Alison M. Winger</name></author><author><name sortKey="Hecker, Arnaud" sort="Hecker, Arnaud" uniqKey="Hecker A" first="Arnaud" last="Hecker">Arnaud Hecker</name></author><author><name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name></author><author><name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name></author><author><name sortKey="Gans, Pierre" sort="Gans, Pierre" uniqKey="Gans P" first="Pierre" last="Gans">Pierre Gans</name></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author><author><name sortKey="Navaza, Alda" sort="Navaza, Alda" uniqKey="Navaza A" first="Alda" last="Navaza">Alda Navaza</name></author><author><name sortKey="Haouz, Ahmed" sort="Haouz, Ahmed" uniqKey="Haouz A" first="Ahmed" last="Haouz">Ahmed Haouz</name></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:22866991</idno><idno type="pmid">22866991</idno><idno type="doi">10.1089/ars.2012.4739</idno><idno type="pmc">PMC3613187</idno><idno type="wicri:Area/Main/Corpus">000817</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000817</idno><idno type="wicri:Area/Main/Curation">000817</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000817</idno><idno type="wicri:Area/Main/Exploration">000817</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?</title><author><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><affiliation wicri:level="1"><nlm:affiliation>Unité Mixte de Recherches 1136 INRA-Lorraine Université, Interactions Arbres-Microorganismes, IFR 110, Faculté des Sciences, Vandoeuvre Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Unité Mixte de Recherches 1136 INRA-Lorraine Université, Interactions Arbres-Microorganismes, IFR 110, Faculté des Sciences, Vandoeuvre Cedex</wicri:regionArea><wicri:noRegion>Vandoeuvre Cedex</wicri:noRegion><wicri:noRegion>Vandoeuvre Cedex</wicri:noRegion></affiliation></author><author><name sortKey="Prosper, Pascalita" sort="Prosper, Pascalita" uniqKey="Prosper P" first="Pascalita" last="Prosper">Pascalita Prosper</name></author><author><name sortKey="Winger, Alison M" sort="Winger, Alison M" uniqKey="Winger A" first="Alison M" last="Winger">Alison M. Winger</name></author><author><name sortKey="Hecker, Arnaud" sort="Hecker, Arnaud" uniqKey="Hecker A" first="Arnaud" last="Hecker">Arnaud Hecker</name></author><author><name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name></author><author><name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name></author><author><name sortKey="Gans, Pierre" sort="Gans, Pierre" uniqKey="Gans P" first="Pierre" last="Gans">Pierre Gans</name></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author><author><name sortKey="Navaza, Alda" sort="Navaza, Alda" uniqKey="Navaza A" first="Alda" last="Navaza">Alda Navaza</name></author><author><name sortKey="Haouz, Ahmed" sort="Haouz, Ahmed" uniqKey="Haouz A" first="Ahmed" last="Haouz">Ahmed Haouz</name></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Catalysis (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Peroxidase (metabolism)</term><term>Peroxiredoxins (chemistry)</term><term>Peroxiredoxins (metabolism)</term><term>Protein Conformation (MeSH)</term><term>Protein Interaction Domains and Motifs (MeSH)</term><term>Protein Multimerization (MeSH)</term><term>Reducing Agents (metabolism)</term><term>Thermotoga maritima (metabolism)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Motifs et domaines d'intéraction protéique (MeSH)</term><term>Multimérisation de protéines (MeSH)</term><term>Myeloperoxidase (métabolisme)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Peroxirédoxines (composition chimique)</term><term>Peroxirédoxines (métabolisme)</term><term>Réducteurs (métabolisme)</term><term>Thermotoga maritima (métabolisme)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxiredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases</term><term>Peroxidase</term><term>Peroxiredoxins</term><term>Reducing Agents</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peroxirédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Thermotoga maritima</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Myeloperoxidase</term><term>Oxidoreductases</term><term>Peroxirédoxines</term><term>Réducteurs</term><term>Thermotoga maritima</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Oxidation-Reduction</term><term>Protein Conformation</term><term>Protein Interaction Domains and Motifs</term><term>Protein Multimerization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Conformation des protéines</term><term>Motifs et domaines d'intéraction protéique</term><term>Multimérisation de protéines</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Three peroxiredoxins (Prxs) were identified in Thermotoga maritima, which possesses neither glutathione nor typical thioredoxins: one of the Prx6 class; one 2-Cys PrxBCP; and a unique hybrid protein containing an N-terminal 1-Cys PrxBCP domain fused to a flavin mononucleotide-containing nitroreductase (Ntr) domain. No peroxidase activity was detected for Prx6, whereas both bacterioferritin comigratory proteins (BCPs) were regenerated by a NADH/thioredoxin reductase/glutaredoxin (Grx)-like system, constituting a unique peroxide removal system. Only two of the three Grx-like proteins were able to support peroxidase activity. The inability of TmGrx1 to regenerate oxidized 2-Cys PrxBCP probably results from the thermodynamically unfavorable difference in their disulfide/dithiol E(m) values, -150 and -315 mV, respectively. Mutagenesis of the Prx-Ntr fusion, combined with kinetic and structural analyses, indicated that electrons are not transferred between its two domains. However, their separate activities could function in a complementary manner, with peroxide originating from the chromate reductase activity of the Ntr domain reduced by the Prx domain.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22866991</PMID><DateCompleted><Year>2013</Year><Month>09</Month><Day>13</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>18</Volume><Issue>13</Issue><PubDate><Year>2013</Year><Month>May</Month><Day>01</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?</ArticleTitle><Pagination><MedlinePgn>1613-22</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2012.4739</ELocationID><Abstract><AbstractText>Three peroxiredoxins (Prxs) were identified in Thermotoga maritima, which possesses neither glutathione nor typical thioredoxins: one of the Prx6 class; one 2-Cys PrxBCP; and a unique hybrid protein containing an N-terminal 1-Cys PrxBCP domain fused to a flavin mononucleotide-containing nitroreductase (Ntr) domain. No peroxidase activity was detected for Prx6, whereas both bacterioferritin comigratory proteins (BCPs) were regenerated by a NADH/thioredoxin reductase/glutaredoxin (Grx)-like system, constituting a unique peroxide removal system. Only two of the three Grx-like proteins were able to support peroxidase activity. The inability of TmGrx1 to regenerate oxidized 2-Cys PrxBCP probably results from the thermodynamically unfavorable difference in their disulfide/dithiol E(m) values, -150 and -315 mV, respectively. Mutagenesis of the Prx-Ntr fusion, combined with kinetic and structural analyses, indicated that electrons are not transferred between its two domains. However, their separate activities could function in a complementary manner, with peroxide originating from the chromate reductase activity of the Ntr domain reduced by the Prx domain.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Couturier</LastName><ForeName>Jérémy</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Unité Mixte de Recherches 1136 INRA-Lorraine Université, Interactions Arbres-Microorganismes, IFR 110, Faculté des Sciences, Vandoeuvre Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Prosper</LastName><ForeName>Pascalita</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Winger</LastName><ForeName>Alison M</ForeName><Initials>AM</Initials></Author><Author ValidYN="Y"><LastName>Hecker</LastName><ForeName>Arnaud</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Hirasawa</LastName><ForeName>Masakazu</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Knaff</LastName><ForeName>David B</ForeName><Initials>DB</Initials></Author><Author ValidYN="Y"><LastName>Gans</LastName><ForeName>Pierre</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Navaza</LastName><ForeName>Alda</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Haouz</LastName><ForeName>Ahmed</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>4EO3</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>09</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019163">Reducing Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.7</RegistryNumber><NameOfSubstance UI="D009195">Peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009195" MajorTopicYN="N">Peroxidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019163" MajorTopicYN="N">Reducing Agents</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020124" MajorTopicYN="N">Thermotoga maritima</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>8</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>8</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>9</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22866991</ArticleId><ArticleId IdType="doi">10.1089/ars.2012.4739</ArticleId><ArticleId IdType="pmc">PMC3613187</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Biochemistry. 2002 Feb 12;41(6):1990-2001</Citation><ArticleIdList><ArticleId IdType="pubmed">11827546</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2004 Mar;134(3):1027-38</Citation><ArticleIdList><ArticleId IdType="pubmed">14976238</ArticleId></ArticleIdList></Reference><Reference><Citation>Environ Microbiol. 2004 Aug;6(8):851-60</Citation><ArticleIdList><ArticleId IdType="pubmed">15250887</ArticleId></ArticleIdList></Reference><Reference><Citation>Free Radic Biol Med. 2005 Jun 1;38(11):1413-21</Citation><ArticleIdList><ArticleId IdType="pubmed">15890615</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2011 Oct 18;50(41):8970-81</Citation><ArticleIdList><ArticleId IdType="pubmed">21910476</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2010 Feb 16;49(6):1319-30</Citation><ArticleIdList><ArticleId IdType="pubmed">20078128</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 2010 Mar;192(5):1370-6</Citation><ArticleIdList><ArticleId IdType="pubmed">20061476</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2011 Aug 1;15(3):795-815</Citation><ArticleIdList><ArticleId IdType="pubmed">20969484</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2009 May 12;48(18):3904-14</Citation><ArticleIdList><ArticleId IdType="pubmed">19298085</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>France</li></country></list><tree><noCountry><name sortKey="Gans, Pierre" sort="Gans, Pierre" uniqKey="Gans P" first="Pierre" last="Gans">Pierre Gans</name><name sortKey="Haouz, Ahmed" sort="Haouz, Ahmed" uniqKey="Haouz A" first="Ahmed" last="Haouz">Ahmed Haouz</name><name sortKey="Hecker, Arnaud" sort="Hecker, Arnaud" uniqKey="Hecker A" first="Arnaud" last="Hecker">Arnaud Hecker</name><name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name><name sortKey="Navaza, Alda" sort="Navaza, Alda" uniqKey="Navaza A" first="Alda" last="Navaza">Alda Navaza</name><name sortKey="Prosper, Pascalita" sort="Prosper, Pascalita" uniqKey="Prosper P" first="Pascalita" last="Prosper">Pascalita Prosper</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Winger, Alison M" sort="Winger, Alison M" uniqKey="Winger A" first="Alison M" last="Winger">Alison M. Winger</name></noCountry><country name="France"><noRegion><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</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 000751 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000751 | 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:22866991
|texte= In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:22866991" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |