Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG.
Identifieur interne : 002356 ( Main/Exploration ); précédent : 002355; suivant : 002357Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG.
Auteurs : Claudio F. Gonzalez [Canada] ; Michael Proudfoot ; Greg Brown ; Yurij Korniyenko ; Hirotada Mori ; Alexei V. Savchenko ; Alexander F. YakuninSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2006.
Descripteurs français
- KwdFr :
- Cinétique (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (enzymologie), Formaldéhyde (métabolisme), Formaldéhyde (toxicité), Hydrolyse (MeSH), Modèles chimiques (MeSH), Modèles moléculaires (MeSH), Protéines Escherichia coli (composition chimique), Saccharomyces cerevisiae (enzymologie), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Thiolester hydrolases (composition chimique).
- MESH :
- composition chimique : Protéines Escherichia coli, Thiolester hydrolases.
- enzymologie : Escherichia coli, Saccharomyces cerevisiae.
- métabolisme : Formaldéhyde.
- toxicité : Formaldéhyde.
- Cinétique, Conformation des protéines, Cristallographie aux rayons X, Données de séquences moléculaires, Hydrolyse, Modèles chimiques, Modèles moléculaires, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Crystallography, X-Ray (MeSH), Escherichia coli (enzymology), Escherichia coli Proteins (chemistry), Formaldehyde (metabolism), Formaldehyde (toxicity), Hydrolysis (MeSH), Kinetics (MeSH), Models, Chemical (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Protein Conformation (MeSH), Saccharomyces cerevisiae (enzymology), Sequence Homology, Amino Acid (MeSH), Thiolester Hydrolases (chemistry).
- MESH :
- chemical , chemistry : Escherichia coli Proteins, Thiolester Hydrolases.
- enzymology : Escherichia coli, Saccharomyces cerevisiae.
- chemical , metabolism : Formaldehyde.
- chemical , toxicity : Formaldehyde.
- Amino Acid Sequence, Crystallography, X-Ray, Hydrolysis, Kinetics, Models, Chemical, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid.
Abstract
The Escherichia coli genes frmB (yaiM) and yeiG encode two uncharacterized proteins that share 54% sequence identity and contain a serine esterase motif. We demonstrated that purified FrmB and YeiG have high carboxylesterase activity against the model substrates, p-nitrophenyl esters of fatty acids (C2-C6) and alpha-naphthyl acetate. However, both proteins had the highest hydrolytic activity toward S-formylglutathione, an intermediate of the glutathione-dependent pathway of formaldehyde detoxification. With this substrate, both proteins had similar affinity (Km = 0.41-0.43 mM), but FrmB was almost 5 times more active. Alanine replacement mutagenesis of YeiG demonstrated that Ser145, Asp233, and His256 are absolutely required for activity, indicating that these residues represent a serine hydrolase catalytic triad in this protein and in other S-formylglutathione hydrolases. This was confirmed by inspecting the crystal structure of the Saccharomyces cerevisiae S-formylglutathione hydrolase YJG8 (Protein Data Bank code 1pv1), which has 45% sequence identity to YeiG. The structure revealed a canonical alpha/beta-hydrolase fold and a classical serine hydrolase catalytic triad (Ser161, His276, Asp241). In E. coli cells, the expression of frmB was stimulated 45-75 times by the addition of formaldehyde to the growth medium, whereas YeiG was found to be a constitutive enzyme. The simultaneous deletion of both frmB and yeiG genes was required to increase the sensitivity of the growth of E. coli cells to formaldehyde, suggesting that both FrmB and YeiG contribute to the detoxification of formaldehyde. Thus, FrmB and YeiG are S-formylglutathione hydrolases with a Ser-His-Asp catalytic triad involved in the detoxification of formaldehyde in E. coli.
DOI: 10.1074/jbc.M600996200
PubMed: 16567800
Affiliations:
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Gonzalez</name><affiliation wicri:level="4"><nlm:affiliation>Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6</wicri:regionArea><orgName type="university">Université de Toronto</orgName><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author><author><name sortKey="Proudfoot, Michael" sort="Proudfoot, Michael" uniqKey="Proudfoot M" first="Michael" last="Proudfoot">Michael Proudfoot</name></author><author><name sortKey="Brown, Greg" sort="Brown, Greg" uniqKey="Brown G" first="Greg" last="Brown">Greg Brown</name></author><author><name sortKey="Korniyenko, Yurij" sort="Korniyenko, Yurij" uniqKey="Korniyenko Y" first="Yurij" last="Korniyenko">Yurij Korniyenko</name></author><author><name sortKey="Mori, Hirotada" sort="Mori, Hirotada" uniqKey="Mori H" first="Hirotada" last="Mori">Hirotada Mori</name></author><author><name sortKey="Savchenko, Alexei V" sort="Savchenko, Alexei V" uniqKey="Savchenko A" first="Alexei V" last="Savchenko">Alexei V. Savchenko</name></author><author><name sortKey="Yakunin, Alexander F" sort="Yakunin, Alexander F" uniqKey="Yakunin A" first="Alexander F" last="Yakunin">Alexander F. Yakunin</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16567800</idno><idno type="pmid">16567800</idno><idno type="doi">10.1074/jbc.M600996200</idno><idno type="wicri:Area/Main/Corpus">002397</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002397</idno><idno type="wicri:Area/Main/Curation">002397</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002397</idno><idno type="wicri:Area/Main/Exploration">002397</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG.</title><author><name sortKey="Gonzalez, Claudio F" sort="Gonzalez, Claudio F" uniqKey="Gonzalez C" first="Claudio F" last="Gonzalez">Claudio F. Gonzalez</name><affiliation wicri:level="4"><nlm:affiliation>Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6</wicri:regionArea><orgName type="university">Université de Toronto</orgName><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author><author><name sortKey="Proudfoot, Michael" sort="Proudfoot, Michael" uniqKey="Proudfoot M" first="Michael" last="Proudfoot">Michael Proudfoot</name></author><author><name sortKey="Brown, Greg" sort="Brown, Greg" uniqKey="Brown G" first="Greg" last="Brown">Greg Brown</name></author><author><name sortKey="Korniyenko, Yurij" sort="Korniyenko, Yurij" uniqKey="Korniyenko Y" first="Yurij" last="Korniyenko">Yurij Korniyenko</name></author><author><name sortKey="Mori, Hirotada" sort="Mori, Hirotada" uniqKey="Mori H" first="Hirotada" last="Mori">Hirotada Mori</name></author><author><name sortKey="Savchenko, Alexei V" sort="Savchenko, Alexei V" uniqKey="Savchenko A" first="Alexei V" last="Savchenko">Alexei V. Savchenko</name></author><author><name sortKey="Yakunin, Alexander F" sort="Yakunin, Alexander F" uniqKey="Yakunin A" first="Alexander F" last="Yakunin">Alexander F. Yakunin</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Escherichia coli (enzymology)</term><term>Escherichia coli Proteins (chemistry)</term><term>Formaldehyde (metabolism)</term><term>Formaldehyde (toxicity)</term><term>Hydrolysis (MeSH)</term><term>Kinetics (MeSH)</term><term>Models, Chemical (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Saccharomyces cerevisiae (enzymology)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Thiolester Hydrolases (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (enzymologie)</term><term>Formaldéhyde (métabolisme)</term><term>Formaldéhyde (toxicité)</term><term>Hydrolyse (MeSH)</term><term>Modèles chimiques (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Protéines Escherichia coli (composition chimique)</term><term>Saccharomyces cerevisiae (enzymologie)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiolester hydrolases (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Escherichia coli Proteins</term><term>Thiolester Hydrolases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines Escherichia coli</term><term>Thiolester hydrolases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Formaldehyde</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Formaldéhyde</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Formaldehyde</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Formaldéhyde</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography, X-Ray</term><term>Hydrolysis</term><term>Kinetics</term><term>Models, Chemical</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Hydrolyse</term><term>Modèles chimiques</term><term>Modèles moléculaires</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Escherichia coli genes frmB (yaiM) and yeiG encode two uncharacterized proteins that share 54% sequence identity and contain a serine esterase motif. We demonstrated that purified FrmB and YeiG have high carboxylesterase activity against the model substrates, p-nitrophenyl esters of fatty acids (C2-C6) and alpha-naphthyl acetate. However, both proteins had the highest hydrolytic activity toward S-formylglutathione, an intermediate of the glutathione-dependent pathway of formaldehyde detoxification. With this substrate, both proteins had similar affinity (Km = 0.41-0.43 mM), but FrmB was almost 5 times more active. Alanine replacement mutagenesis of YeiG demonstrated that Ser145, Asp233, and His256 are absolutely required for activity, indicating that these residues represent a serine hydrolase catalytic triad in this protein and in other S-formylglutathione hydrolases. This was confirmed by inspecting the crystal structure of the Saccharomyces cerevisiae S-formylglutathione hydrolase YJG8 (Protein Data Bank code 1pv1), which has 45% sequence identity to YeiG. The structure revealed a canonical alpha/beta-hydrolase fold and a classical serine hydrolase catalytic triad (Ser161, His276, Asp241). In E. coli cells, the expression of frmB was stimulated 45-75 times by the addition of formaldehyde to the growth medium, whereas YeiG was found to be a constitutive enzyme. The simultaneous deletion of both frmB and yeiG genes was required to increase the sensitivity of the growth of E. coli cells to formaldehyde, suggesting that both FrmB and YeiG contribute to the detoxification of formaldehyde. Thus, FrmB and YeiG are S-formylglutathione hydrolases with a Ser-His-Asp catalytic triad involved in the detoxification of formaldehyde in E. coli.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16567800</PMID><DateCompleted><Year>2006</Year><Month>07</Month><Day>21</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>281</Volume><Issue>20</Issue><PubDate><Year>2006</Year><Month>May</Month><Day>19</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG.</ArticleTitle><Pagination><MedlinePgn>14514-22</MedlinePgn></Pagination><Abstract><AbstractText>The Escherichia coli genes frmB (yaiM) and yeiG encode two uncharacterized proteins that share 54% sequence identity and contain a serine esterase motif. We demonstrated that purified FrmB and YeiG have high carboxylesterase activity against the model substrates, p-nitrophenyl esters of fatty acids (C2-C6) and alpha-naphthyl acetate. However, both proteins had the highest hydrolytic activity toward S-formylglutathione, an intermediate of the glutathione-dependent pathway of formaldehyde detoxification. With this substrate, both proteins had similar affinity (Km = 0.41-0.43 mM), but FrmB was almost 5 times more active. Alanine replacement mutagenesis of YeiG demonstrated that Ser145, Asp233, and His256 are absolutely required for activity, indicating that these residues represent a serine hydrolase catalytic triad in this protein and in other S-formylglutathione hydrolases. This was confirmed by inspecting the crystal structure of the Saccharomyces cerevisiae S-formylglutathione hydrolase YJG8 (Protein Data Bank code 1pv1), which has 45% sequence identity to YeiG. The structure revealed a canonical alpha/beta-hydrolase fold and a classical serine hydrolase catalytic triad (Ser161, His276, Asp241). In E. coli cells, the expression of frmB was stimulated 45-75 times by the addition of formaldehyde to the growth medium, whereas YeiG was found to be a constitutive enzyme. The simultaneous deletion of both frmB and yeiG genes was required to increase the sensitivity of the growth of E. coli cells to formaldehyde, suggesting that both FrmB and YeiG contribute to the detoxification of formaldehyde. Thus, FrmB and YeiG are S-formylglutathione hydrolases with a Ser-His-Asp catalytic triad involved in the detoxification of formaldehyde in E. coli.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gonzalez</LastName><ForeName>Claudio F</ForeName><Initials>CF</Initials><AffiliationInfo><Affiliation>Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Proudfoot</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Brown</LastName><ForeName>Greg</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Korniyenko</LastName><ForeName>Yurij</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Mori</LastName><ForeName>Hirotada</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Savchenko</LastName><ForeName>Alexei V</ForeName><Initials>AV</Initials></Author><Author ValidYN="Y"><LastName>Yakunin</LastName><ForeName>Alexander F</ForeName><Initials>AF</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM62414-01</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>03</Month><Day>27</Day></ArticleDate></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="D029968">Escherichia coli Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>1HG84L3525</RegistryNumber><NameOfSubstance UI="D005557">Formaldehyde</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.2.-</RegistryNumber><NameOfSubstance UI="D013869">Thiolester Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.2.12</RegistryNumber><NameOfSubstance UI="C511806">FrmB protein, E coli</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.2.12</RegistryNumber><NameOfSubstance UI="C511807">YeiG protein, E coli</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.2.12</RegistryNumber><NameOfSubstance UI="C020149">s-formylglutathione hydrolase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029968" MajorTopicYN="N">Escherichia coli Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005557" MajorTopicYN="N">Formaldehyde</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013869" MajorTopicYN="N">Thiolester Hydrolases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>3</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>7</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>3</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16567800</ArticleId><ArticleId IdType="pii">M600996200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M600996200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country><region><li>Ontario</li></region><settlement><li>Toronto</li></settlement><orgName><li>Université de Toronto</li></orgName></list><tree><noCountry><name sortKey="Brown, Greg" sort="Brown, Greg" uniqKey="Brown G" first="Greg" last="Brown">Greg Brown</name><name sortKey="Korniyenko, Yurij" sort="Korniyenko, Yurij" uniqKey="Korniyenko Y" first="Yurij" last="Korniyenko">Yurij Korniyenko</name><name sortKey="Mori, Hirotada" sort="Mori, Hirotada" uniqKey="Mori H" first="Hirotada" last="Mori">Hirotada Mori</name><name sortKey="Proudfoot, Michael" sort="Proudfoot, Michael" uniqKey="Proudfoot M" first="Michael" last="Proudfoot">Michael Proudfoot</name><name sortKey="Savchenko, Alexei V" sort="Savchenko, Alexei V" uniqKey="Savchenko A" first="Alexei V" last="Savchenko">Alexei V. Savchenko</name><name sortKey="Yakunin, Alexander F" sort="Yakunin, Alexander F" uniqKey="Yakunin A" first="Alexander F" last="Yakunin">Alexander F. Yakunin</name></noCountry><country name="Canada"><region name="Ontario"><name sortKey="Gonzalez, Claudio F" sort="Gonzalez, Claudio F" uniqKey="Gonzalez C" first="Claudio F" last="Gonzalez">Claudio F. Gonzalez</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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