Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases.
Identifieur interne : 000164 ( Main/Exploration ); précédent : 000163; suivant : 000165Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases.
Auteurs : Sandra Acebes [Espagne] ; Francisco J. Ruiz-Due As [Espagne] ; Mario Toubes [Espagne] ; Veronica Sáez-Jiménez [Espagne] ; Marta Pérez-Boada [Espagne] ; M Fátima Lucas [Espagne] ; Angel T. Martínez [Espagne] ; Victor Guallar [Espagne]Source :
- The journal of physical chemistry. B [ 1520-5207 ] ; 2017.
Descripteurs français
- KwdFr :
- Lignine (métabolisme), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Pleurotus (composition chimique), Pleurotus (enzymologie), Pleurotus (génétique), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH), Transport d'électrons (MeSH).
- MESH :
- composition chimique : Peroxidases, Pleurotus.
- enzymologie : Pleurotus.
- génétique : Peroxidases, Pleurotus.
- métabolisme : Lignine, Peroxidases.
- Modèles moléculaires, Mutagenèse dirigée, Oxydoréduction, Spécificité du substrat, Séquence d'acides aminés, Transport d'électrons.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Electron Transport (MeSH), Lignin (metabolism), Models, Molecular (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Pleurotus (chemistry), Pleurotus (enzymology), Pleurotus (genetics), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Peroxidases.
- chemical , genetics : Peroxidases.
- chemical , metabolism : Lignin, Peroxidases.
- chemistry : Pleurotus.
- enzymology : Pleurotus.
- genetics : Pleurotus.
- Amino Acid Sequence, Electron Transport, Models, Molecular, Mutagenesis, Site-Directed, Oxidation-Reduction, Substrate Specificity.
Abstract
Combining a computational analysis with site-directed mutagenesis, we have studied the long-range electron transfer pathway in versatile and lignin peroxidases, two enzymes of biotechnological interest that play a key role for fungal degradation of the bulky lignin molecule in plant biomass. The in silico study established two possible electron transfer routes starting at the surface tryptophan residue previously identified as responsible for oxidation of the bulky lignin polymer. Moreover, in both enzymes, a second buried tryptophan residue appears as a top electron transfer carrier, indicating the prevalence of one pathway. Site-directed mutagenesis of versatile peroxidase (from Pleurotus eryngii) allowed us to corroborate the computational analysis and the role played by the buried tryptophan (Trp244) and a neighbor phenylalanine residue (Phe198), together with the surface tryptophan, in the electron transfer. These three aromatic residues are highly conserved in all the sequences analyzed (up to a total of 169). The importance of the surface (Trp171) and buried (Trp251) tryptophan residues in lignin peroxidase has been also confirmed by directed mutagenesis of the Phanerochaete chrysosporium enzyme. Overall, the combined procedure identifies analogous electron transfer pathways in the long-range oxidation mechanism for both ligninolytic peroxidases, constituting a good example of how computational analysis avoids making extensive trial-error mutagenic experiments.
DOI: 10.1021/acs.jpcb.7b00835
PubMed: 28375014
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Ruiz-Due As</name><affiliation wicri:level="2"><nlm:affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Toubes, Mario" sort="Toubes, Mario" uniqKey="Toubes M" first="Mario" last="Toubes">Mario Toubes</name><affiliation wicri:level="2"><nlm:affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Saez Jimenez, Veronica" sort="Saez Jimenez, Veronica" uniqKey="Saez Jimenez V" first="Veronica" last="Sáez-Jiménez">Veronica Sáez-Jiménez</name><affiliation wicri:level="2"><nlm:affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Perez Boada, Marta" sort="Perez Boada, Marta" uniqKey="Perez Boada M" first="Marta" last="Pérez-Boada">Marta Pérez-Boada</name><affiliation wicri:level="2"><nlm:affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Lucas, M Fatima" sort="Lucas, M Fatima" uniqKey="Lucas M" first="M Fátima" last="Lucas">M Fátima Lucas</name><affiliation wicri:level="2"><nlm:affiliation>Barcelona Supercomputing Center, Joint BSC-CRG-IRB Research Program in Computational Biology , Jordi Girona 29, E-08034 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Barcelona Supercomputing Center, Joint BSC-CRG-IRB Research Program in Computational Biology , Jordi Girona 29, E-08034 Barcelona</wicri:regionArea><placeName><region nuts="2" type="communauté">Catalogne</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>Anaxomics Biotech , Balmes 89, 08008 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Anaxomics Biotech , Balmes 89, 08008 Barcelona</wicri:regionArea><placeName><region nuts="2" type="communauté">Catalogne</region></placeName></affiliation></author><author><name sortKey="Martinez, Angel T" sort="Martinez, Angel T" uniqKey="Martinez A" first="Angel T" last="Martínez">Angel T. Martínez</name><affiliation wicri:level="2"><nlm:affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Guallar, Victor" sort="Guallar, Victor" uniqKey="Guallar V" first="Victor" last="Guallar">Victor Guallar</name><affiliation wicri:level="2"><nlm:affiliation>Barcelona Supercomputing Center, Joint BSC-CRG-IRB Research Program in Computational Biology , Jordi Girona 29, E-08034 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Barcelona Supercomputing Center, Joint BSC-CRG-IRB Research Program in Computational Biology , Jordi Girona 29, E-08034 Barcelona</wicri:regionArea><placeName><region nuts="2" type="communauté">Catalogne</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>ICREA , Passeig Lluís Companys 23, E-08010 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>ICREA , Passeig Lluís Companys 23, E-08010 Barcelona</wicri:regionArea><placeName><region nuts="2" type="communauté">Catalogne</region></placeName></affiliation></author></analytic><series><title level="j">The journal of physical chemistry. B</title><idno type="eISSN">1520-5207</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Electron Transport (MeSH)</term><term>Lignin (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Pleurotus (chemistry)</term><term>Pleurotus (enzymology)</term><term>Pleurotus (genetics)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Lignine (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Pleurotus (composition chimique)</term><term>Pleurotus (enzymologie)</term><term>Pleurotus (génétique)</term><term>Spécificité du substrat (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peroxidases</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peroxidases</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Electron Transport</term><term>Models, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Oxidation-Reduction</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Oxydoréduction</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Combining a computational analysis with site-directed mutagenesis, we have studied the long-range electron transfer pathway in versatile and lignin peroxidases, two enzymes of biotechnological interest that play a key role for fungal degradation of the bulky lignin molecule in plant biomass. The in silico study established two possible electron transfer routes starting at the surface tryptophan residue previously identified as responsible for oxidation of the bulky lignin polymer. Moreover, in both enzymes, a second buried tryptophan residue appears as a top electron transfer carrier, indicating the prevalence of one pathway. Site-directed mutagenesis of versatile peroxidase (from Pleurotus eryngii) allowed us to corroborate the computational analysis and the role played by the buried tryptophan (Trp244) and a neighbor phenylalanine residue (Phe198), together with the surface tryptophan, in the electron transfer. These three aromatic residues are highly conserved in all the sequences analyzed (up to a total of 169). The importance of the surface (Trp171) and buried (Trp251) tryptophan residues in lignin peroxidase has been also confirmed by directed mutagenesis of the Phanerochaete chrysosporium enzyme. Overall, the combined procedure identifies analogous electron transfer pathways in the long-range oxidation mechanism for both ligninolytic peroxidases, constituting a good example of how computational analysis avoids making extensive trial-error mutagenic experiments.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28375014</PMID><DateCompleted><Year>2018</Year><Month>05</Month><Day>03</Day></DateCompleted><DateRevised><Year>2018</Year><Month>05</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5207</ISSN><JournalIssue CitedMedium="Internet"><Volume>121</Volume><Issue>16</Issue><PubDate><Year>2017</Year><Month>04</Month><Day>27</Day></PubDate></JournalIssue><Title>The journal of physical chemistry. B</Title><ISOAbbreviation>J Phys Chem B</ISOAbbreviation></Journal><ArticleTitle>Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases.</ArticleTitle><Pagination><MedlinePgn>3946-3954</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.jpcb.7b00835</ELocationID><Abstract><AbstractText>Combining a computational analysis with site-directed mutagenesis, we have studied the long-range electron transfer pathway in versatile and lignin peroxidases, two enzymes of biotechnological interest that play a key role for fungal degradation of the bulky lignin molecule in plant biomass. The in silico study established two possible electron transfer routes starting at the surface tryptophan residue previously identified as responsible for oxidation of the bulky lignin polymer. Moreover, in both enzymes, a second buried tryptophan residue appears as a top electron transfer carrier, indicating the prevalence of one pathway. Site-directed mutagenesis of versatile peroxidase (from Pleurotus eryngii) allowed us to corroborate the computational analysis and the role played by the buried tryptophan (Trp244) and a neighbor phenylalanine residue (Phe198), together with the surface tryptophan, in the electron transfer. These three aromatic residues are highly conserved in all the sequences analyzed (up to a total of 169). The importance of the surface (Trp171) and buried (Trp251) tryptophan residues in lignin peroxidase has been also confirmed by directed mutagenesis of the Phanerochaete chrysosporium enzyme. Overall, the combined procedure identifies analogous electron transfer pathways in the long-range oxidation mechanism for both ligninolytic peroxidases, constituting a good example of how computational analysis avoids making extensive trial-error mutagenic experiments.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Acebes</LastName><ForeName>Sandra</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Barcelona Supercomputing Center, Joint BSC-CRG-IRB Research Program in Computational Biology , Jordi Girona 29, E-08034 Barcelona, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ruiz-Dueñas</LastName><ForeName>Francisco J</ForeName><Initials>FJ</Initials><AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Toubes</LastName><ForeName>Mario</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sáez-Jiménez</LastName><ForeName>Veronica</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pérez-Boada</LastName><ForeName>Marta</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lucas</LastName><ForeName>M Fátima</ForeName><Initials>MF</Initials><AffiliationInfo><Affiliation>Barcelona Supercomputing Center, Joint BSC-CRG-IRB Research Program in Computational Biology , Jordi Girona 29, E-08034 Barcelona, Spain.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Anaxomics Biotech , Balmes 89, 08008 Barcelona, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>Angel T</ForeName><Initials>AT</Initials><Identifier Source="ORCID">0000-0002-1584-2863</Identifier><AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guallar</LastName><ForeName>Victor</ForeName><Initials>V</Initials><Identifier Source="ORCID">0000-0002-4580-1114</Identifier><AffiliationInfo><Affiliation>Barcelona Supercomputing Center, Joint BSC-CRG-IRB Research Program in Computational Biology , Jordi Girona 29, E-08034 Barcelona, Spain.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>ICREA , Passeig Lluís Companys 23, E-08010 Barcelona, Spain.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>04</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Phys Chem B</MedlineTA><NlmUniqueID>101157530</NlmUniqueID><ISSNLinking>1520-5207</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020076" MajorTopicYN="N">Pleurotus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>4</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>5</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>4</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28375014</ArticleId><ArticleId IdType="doi">10.1021/acs.jpcb.7b00835</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Catalogne</li><li>Communauté de Madrid</li></region></list><tree><country name="Espagne"><region name="Catalogne"><name sortKey="Acebes, Sandra" sort="Acebes, Sandra" uniqKey="Acebes S" first="Sandra" last="Acebes">Sandra Acebes</name></region><name sortKey="Guallar, Victor" sort="Guallar, Victor" uniqKey="Guallar V" first="Victor" last="Guallar">Victor Guallar</name><name sortKey="Guallar, Victor" sort="Guallar, Victor" uniqKey="Guallar V" first="Victor" last="Guallar">Victor Guallar</name><name sortKey="Lucas, M Fatima" sort="Lucas, M Fatima" uniqKey="Lucas M" first="M Fátima" last="Lucas">M Fátima Lucas</name><name sortKey="Lucas, M Fatima" sort="Lucas, M Fatima" uniqKey="Lucas M" first="M Fátima" last="Lucas">M Fátima Lucas</name><name sortKey="Martinez, Angel T" sort="Martinez, Angel T" uniqKey="Martinez A" first="Angel T" last="Martínez">Angel T. Martínez</name><name sortKey="Perez Boada, Marta" sort="Perez Boada, Marta" uniqKey="Perez Boada M" first="Marta" last="Pérez-Boada">Marta Pérez-Boada</name><name sortKey="Ruiz Due As, Francisco J" sort="Ruiz Due As, Francisco J" uniqKey="Ruiz Due As F" first="Francisco J" last="Ruiz-Due As">Francisco J. Ruiz-Due As</name><name sortKey="Saez Jimenez, Veronica" sort="Saez Jimenez, Veronica" uniqKey="Saez Jimenez V" first="Veronica" last="Sáez-Jiménez">Veronica Sáez-Jiménez</name><name sortKey="Toubes, Mario" sort="Toubes, Mario" uniqKey="Toubes M" first="Mario" last="Toubes">Mario Toubes</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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