Identification of Tyr74 and Tyr177 as substrate oxidation sites in cationic cell wall-bound peroxidase from Populus alba L.
Identifieur interne : 002A38 ( Main/Exploration ); précédent : 002A37; suivant : 002A39Identification of Tyr74 and Tyr177 as substrate oxidation sites in cationic cell wall-bound peroxidase from Populus alba L.
Auteurs : Jun Shigeto [Japon] ; Yoshitaka Itoh ; Yuji Tsutsumi ; Ryuichiro KondoSource :
- The FEBS journal [ 1742-4658 ] ; 2012.
Descripteurs français
- KwdFr :
- Biocatalyse (MeSH), Domaine catalytique (MeSH), Guaïacol (métabolisme), Hydrazones (métabolisme), Lignine (métabolisme), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), Oxydoréduction (MeSH), Paroi cellulaire (enzymologie), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Populus (enzymologie), Propriétés de surface (MeSH), Protéines mutantes (composition chimique), Protéines mutantes (métabolisme), Protéines recombinantes (métabolisme), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéines végétales (métabolisme), Pyrogallol (analogues et dérivés), Pyrogallol (métabolisme), Repliement des protéines (MeSH), Spécificité du substrat (MeSH), Substitution d'acide aminé (MeSH), Tyrosine (composition chimique).
- MESH :
- analogues et dérivés : Pyrogallol.
- composition chimique : Peroxidases, Protéines mutantes, Protéines végétales, Tyrosine.
- enzymologie : Paroi cellulaire, Populus.
- génétique : Peroxidases, Protéines végétales.
- métabolisme : Guaïacol, Hydrazones, Lignine, Peroxidases, Protéines mutantes, Protéines recombinantes, Protéines végétales, Pyrogallol.
- Biocatalyse, Domaine catalytique, Modèles moléculaires, Mutagenèse dirigée, Oxydoréduction, Propriétés de surface, Repliement des protéines, Spécificité du substrat, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Amino Acid Substitution (MeSH), Biocatalysis (MeSH), Catalytic Domain (MeSH), Cell Wall (enzymology), Guaiacol (metabolism), Hydrazones (metabolism), Lignin (metabolism), Models, Molecular (MeSH), Mutagenesis, Site-Directed (MeSH), Mutant Proteins (chemistry), Mutant Proteins (metabolism), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (enzymology), Protein Refolding (MeSH), Pyrogallol (analogs & derivatives), Pyrogallol (metabolism), Recombinant Proteins (metabolism), Substrate Specificity (MeSH), Surface Properties (MeSH), Tyrosine (chemistry).
- MESH :
- chemical , analogs & derivatives : Pyrogallol.
- chemical , chemistry : Mutant Proteins, Peroxidases, Plant Proteins, Tyrosine.
- chemical , genetics : Peroxidases, Plant Proteins.
- chemical , metabolism : Guaiacol, Hydrazones, Lignin, Mutant Proteins, Peroxidases, Plant Proteins, Pyrogallol, Recombinant Proteins.
- enzymology : Cell Wall, Populus.
- Amino Acid Substitution, Biocatalysis, Catalytic Domain, Models, Molecular, Mutagenesis, Site-Directed, Oxidation-Reduction, Protein Refolding, Substrate Specificity, Surface Properties.
Abstract
Cationic cell wall-bound peroxidase (CWPO-C) has the capability to oxidize sinapyl alcohol, ferrocytochrome c, and synthetic lignin polymers, unlike most peroxidases that have been characterized in flowering plants, such as horseradish peroxidase and Arabidopsis thaliana peroxidase A2. It has been suggested that the oxidation site is located on the CWPO-C surface, and homology modeling and chemically modified CWPO-C studies suggest that Tyr74 and/or Tyr177 are possible participants in the catalytic site. The present study clarifies the importance of these Tyr residues for substrate oxidation, using recombinant CWPO-C and recombinant mutant CWPO-C with phenylalanine substitution(s) for tyrosine. Such recombinant proteins, produced in Escherichia coli as inclusion bodies, were successfully refolded to yield the active form, and purified recombinant protein solutions exhibited typical spectra of high-spin ferric protein and displayed H(2) O(2) -dependent oxidation of guaiacol, 2,6-dimethoxyphenol, and syringaldazine. Measurement of peroxidase activity with these guaiacyl and syringyl compounds as reducing substrates indicated that a single mutation, Y74F or Y177F, resulted in substantial loss of oxidation activity (∼ 40-60% and 82%, respectively). Also, over 95% of the oxidation activity was lost with a double mutation, Y74F/Y177F. These results indicated that Tyr74 and Tyr177, rather than the heme pocket, play a central role in the oxidation of these substrates. This is the first report of active residues on an enzyme surface being identified in a plant peroxidase. This study also suggests that sinapyl alcohol incorporation into lignin is performed by a peroxidase that generates Tyr radicals on its surface.
DOI: 10.1111/j.1742-4658.2011.08429.x
PubMed: 22099451
Affiliations:
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Itoh</name></author><author><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name></author><author><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22099451</idno><idno type="pmid">22099451</idno><idno type="doi">10.1111/j.1742-4658.2011.08429.x</idno><idno type="wicri:Area/Main/Corpus">002C25</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002C25</idno><idno type="wicri:Area/Main/Curation">002C25</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002C25</idno><idno type="wicri:Area/Main/Exploration">002C25</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Identification of Tyr74 and Tyr177 as substrate oxidation sites in cationic cell wall-bound peroxidase from Populus alba L.</title><author><name sortKey="Shigeto, Jun" sort="Shigeto, Jun" uniqKey="Shigeto J" first="Jun" last="Shigeto">Jun Shigeto</name><affiliation wicri:level="4"><nlm:affiliation>Department of Forest and Forest Products Sciences, Kyushu University, Fukuoka, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Forest and Forest Products Sciences, Kyushu University, Fukuoka</wicri:regionArea><orgName type="university">Université de Kyūshū</orgName><placeName><settlement type="city">Fukuoka</settlement><region type="province">Kyūshū</region><region type="prefecture">Préfecture de Fukuoka</region></placeName></affiliation></author><author><name sortKey="Itoh, Yoshitaka" sort="Itoh, Yoshitaka" uniqKey="Itoh Y" first="Yoshitaka" last="Itoh">Yoshitaka Itoh</name></author><author><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name></author><author><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name></author></analytic><series><title level="j">The FEBS journal</title><idno type="eISSN">1742-4658</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution (MeSH)</term><term>Biocatalysis (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Cell Wall (enzymology)</term><term>Guaiacol (metabolism)</term><term>Hydrazones (metabolism)</term><term>Lignin (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Mutant Proteins (chemistry)</term><term>Mutant Proteins (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (metabolism)</term><term>Populus (enzymology)</term><term>Protein Refolding (MeSH)</term><term>Pyrogallol (analogs & derivatives)</term><term>Pyrogallol (metabolism)</term><term>Recombinant Proteins (metabolism)</term><term>Substrate Specificity (MeSH)</term><term>Surface Properties (MeSH)</term><term>Tyrosine (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biocatalyse (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Guaïacol (métabolisme)</term><term>Hydrazones (métabolisme)</term><term>Lignine (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Paroi cellulaire (enzymologie)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Populus (enzymologie)</term><term>Propriétés de surface (MeSH)</term><term>Protéines mutantes (composition chimique)</term><term>Protéines mutantes (métabolisme)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (métabolisme)</term><term>Pyrogallol (analogues et dérivés)</term><term>Pyrogallol (métabolisme)</term><term>Repliement des protéines (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Substitution d'acide aminé (MeSH)</term><term>Tyrosine (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Pyrogallol</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Mutant Proteins</term><term>Peroxidases</term><term>Plant Proteins</term><term>Tyrosine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" 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végétales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Guaïacol</term><term>Hydrazones</term><term>Lignine</term><term>Peroxidases</term><term>Protéines mutantes</term><term>Protéines recombinantes</term><term>Protéines végétales</term><term>Pyrogallol</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Biocatalysis</term><term>Catalytic Domain</term><term>Models, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Oxidation-Reduction</term><term>Protein Refolding</term><term>Substrate Specificity</term><term>Surface Properties</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biocatalyse</term><term>Domaine catalytique</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Oxydoréduction</term><term>Propriétés de surface</term><term>Repliement des protéines</term><term>Spécificité du substrat</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cationic cell wall-bound peroxidase (CWPO-C) has the capability to oxidize sinapyl alcohol, ferrocytochrome c, and synthetic lignin polymers, unlike most peroxidases that have been characterized in flowering plants, such as horseradish peroxidase and Arabidopsis thaliana peroxidase A2. It has been suggested that the oxidation site is located on the CWPO-C surface, and homology modeling and chemically modified CWPO-C studies suggest that Tyr74 and/or Tyr177 are possible participants in the catalytic site. The present study clarifies the importance of these Tyr residues for substrate oxidation, using recombinant CWPO-C and recombinant mutant CWPO-C with phenylalanine substitution(s) for tyrosine. Such recombinant proteins, produced in Escherichia coli as inclusion bodies, were successfully refolded to yield the active form, and purified recombinant protein solutions exhibited typical spectra of high-spin ferric protein and displayed H(2) O(2) -dependent oxidation of guaiacol, 2,6-dimethoxyphenol, and syringaldazine. Measurement of peroxidase activity with these guaiacyl and syringyl compounds as reducing substrates indicated that a single mutation, Y74F or Y177F, resulted in substantial loss of oxidation activity (∼ 40-60% and 82%, respectively). Also, over 95% of the oxidation activity was lost with a double mutation, Y74F/Y177F. These results indicated that Tyr74 and Tyr177, rather than the heme pocket, play a central role in the oxidation of these substrates. This is the first report of active residues on an enzyme surface being identified in a plant peroxidase. This study also suggests that sinapyl alcohol incorporation into lignin is performed by a peroxidase that generates Tyr radicals on its surface.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22099451</PMID><DateCompleted><Year>2012</Year><Month>03</Month><Day>06</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1742-4658</ISSN><JournalIssue CitedMedium="Internet"><Volume>279</Volume><Issue>2</Issue><PubDate><Year>2012</Year><Month>Jan</Month></PubDate></JournalIssue><Title>The FEBS journal</Title><ISOAbbreviation>FEBS J</ISOAbbreviation></Journal><ArticleTitle>Identification of Tyr74 and Tyr177 as substrate oxidation sites in cationic cell wall-bound peroxidase from Populus alba L.</ArticleTitle><Pagination><MedlinePgn>348-57</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1742-4658.2011.08429.x</ELocationID><Abstract><AbstractText>Cationic cell wall-bound peroxidase (CWPO-C) has the capability to oxidize sinapyl alcohol, ferrocytochrome c, and synthetic lignin polymers, unlike most peroxidases that have been characterized in flowering plants, such as horseradish peroxidase and Arabidopsis thaliana peroxidase A2. It has been suggested that the oxidation site is located on the CWPO-C surface, and homology modeling and chemically modified CWPO-C studies suggest that Tyr74 and/or Tyr177 are possible participants in the catalytic site. The present study clarifies the importance of these Tyr residues for substrate oxidation, using recombinant CWPO-C and recombinant mutant CWPO-C with phenylalanine substitution(s) for tyrosine. Such recombinant proteins, produced in Escherichia coli as inclusion bodies, were successfully refolded to yield the active form, and purified recombinant protein solutions exhibited typical spectra of high-spin ferric protein and displayed H(2) O(2) -dependent oxidation of guaiacol, 2,6-dimethoxyphenol, and syringaldazine. Measurement of peroxidase activity with these guaiacyl and syringyl compounds as reducing substrates indicated that a single mutation, Y74F or Y177F, resulted in substantial loss of oxidation activity (∼ 40-60% and 82%, respectively). Also, over 95% of the oxidation activity was lost with a double mutation, Y74F/Y177F. These results indicated that Tyr74 and Tyr177, rather than the heme pocket, play a central role in the oxidation of these substrates. This is the first report of active residues on an enzyme surface being identified in a plant peroxidase. This study also suggests that sinapyl alcohol incorporation into lignin is performed by a peroxidase that generates Tyr radicals on its surface.</AbstractText><CopyrightInformation>© 2011 The Authors Journal compilation © 2011 FEBS.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shigeto</LastName><ForeName>Jun</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Forest and Forest Products Sciences, Kyushu University, Fukuoka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Itoh</LastName><ForeName>Yoshitaka</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Tsutsumi</LastName><ForeName>Yuji</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Kondo</LastName><ForeName>Ryuichiro</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>12</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS J</MedlineTA><NlmUniqueID>101229646</NlmUniqueID><ISSNLinking>1742-464X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006835">Hydrazones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050505">Mutant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>01Y4A2QXY0</RegistryNumber><NameOfSubstance UI="D011748">Pyrogallol</NameOfSubstance></Chemical><Chemical><RegistryNumber>14414-32-5</RegistryNumber><NameOfSubstance UI="C009370">syringaldazine</NameOfSubstance></Chemical><Chemical><RegistryNumber>42HK56048U</RegistryNumber><NameOfSubstance UI="D014443">Tyrosine</NameOfSubstance></Chemical><Chemical><RegistryNumber>4UQT464H8K</RegistryNumber><NameOfSubstance UI="C010120">pyrogallol 1,3-dimethyl ether</NameOfSubstance></Chemical><Chemical><RegistryNumber>6JKA7MAH9C</RegistryNumber><NameOfSubstance UI="D006139">Guaiacol</NameOfSubstance></Chemical><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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055162" MajorTopicYN="N">Biocatalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="Y">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002473" MajorTopicYN="N">Cell Wall</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006139" MajorTopicYN="N">Guaiacol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006835" MajorTopicYN="N">Hydrazones</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></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="D050505" MajorTopicYN="N">Mutant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058849" MajorTopicYN="N">Protein Refolding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011748" MajorTopicYN="N">Pyrogallol</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013499" MajorTopicYN="N">Surface Properties</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014443" MajorTopicYN="N">Tyrosine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>11</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>11</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>3</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22099451</ArticleId><ArticleId IdType="doi">10.1111/j.1742-4658.2011.08429.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Kyūshū</li><li>Préfecture de Fukuoka</li></region><settlement><li>Fukuoka</li></settlement><orgName><li>Université de Kyūshū</li></orgName></list><tree><noCountry><name sortKey="Itoh, Yoshitaka" sort="Itoh, Yoshitaka" uniqKey="Itoh Y" first="Yoshitaka" last="Itoh">Yoshitaka Itoh</name><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name></noCountry><country name="Japon"><region name="Kyūshū"><name sortKey="Shigeto, Jun" sort="Shigeto, Jun" uniqKey="Shigeto J" first="Jun" last="Shigeto">Jun Shigeto</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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