Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: evidence for a dinuclear copper center of type 3 and spectroscopic similarities to tyrosinase and hemocyanin.
Identifieur interne : 004866 ( Main/Exploration ); précédent : 004865; suivant : 004867Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: evidence for a dinuclear copper center of type 3 and spectroscopic similarities to tyrosinase and hemocyanin.
Auteurs : A. Rompel [Allemagne] ; H. Fischer ; D. Meiwes ; K. Büldt-Karentzopoulos ; R. Dillinger ; F. Tuczek ; H. Witzel ; B. KrebsSource :
- Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [ 0949-8257 ] ; 1999.
Descripteurs français
- KwdFr :
- Analyse spectrale Raman (MeSH), Antienzymes (pharmacologie), Arbres (enzymologie), Catechol oxidase (composition chimique), Catechol oxidase (isolement et purification), Catechol oxidase (métabolisme), Catéchols (métabolisme), Concentration en ions d'hydrogène (MeSH), Cuivre (métabolisme), Cyanures (pharmacologie), Hémocyanine (composition chimique), Masse moléculaire (MeSH), Monophenol monooxygenase (composition chimique), Phényl-thiourée (pharmacologie), Plantes (enzymologie), Sites de fixation (MeSH), Spectrophotométrie UV (MeSH), Spectrophotométrie atomique (MeSH), Spectroscopie de résonance de spin électronique (MeSH).
- MESH :
- composition chimique : Catechol oxidase, Hémocyanine, Monophenol monooxygenase.
- enzymologie : Arbres, Plantes.
- isolement et purification : Catechol oxidase.
- métabolisme : Catechol oxidase, Catéchols, Cuivre.
- pharmacologie : Antienzymes, Cyanures, Phényl-thiourée.
- Analyse spectrale Raman, Concentration en ions d'hydrogène, Masse moléculaire, Sites de fixation, Spectrophotométrie UV, Spectrophotométrie atomique, Spectroscopie de résonance de spin électronique.
English descriptors
- KwdEn :
- Binding Sites (MeSH), Catechol Oxidase (chemistry), Catechol Oxidase (isolation & purification), Catechol Oxidase (metabolism), Catechols (metabolism), Copper (metabolism), Cyanides (pharmacology), Electron Spin Resonance Spectroscopy (MeSH), Enzyme Inhibitors (pharmacology), Hemocyanins (chemistry), Hydrogen-Ion Concentration (MeSH), Molecular Weight (MeSH), Monophenol Monooxygenase (chemistry), Phenylthiourea (pharmacology), Plants (enzymology), Spectrophotometry, Atomic (MeSH), Spectrophotometry, Ultraviolet (MeSH), Spectrum Analysis, Raman (MeSH), Trees (enzymology).
- MESH :
- chemical , chemistry : Catechol Oxidase, Hemocyanins, Monophenol Monooxygenase.
- chemical , isolation & purification : Catechol Oxidase.
- chemical , metabolism : Catechol Oxidase, Catechols, Copper.
- chemical , pharmacology : Cyanides, Enzyme Inhibitors, Phenylthiourea.
- enzymology : Plants, Trees.
- Binding Sites, Electron Spin Resonance Spectroscopy, Hydrogen-Ion Concentration, Molecular Weight, Spectrophotometry, Atomic, Spectrophotometry, Ultraviolet, Spectrum Analysis, Raman.
Abstract
We purified two catechol oxidases from Lycopus europaeus and Populus nigra which only catalyze the oxidation of catechols to quinones without hydroxylating tyrosine. The molecular mass of the Lycopus enzyme was determined to 39,800 Da and the mass of the Populus enzyme was determined to 56,050 Da. Both catechol oxidases are inhibited by thiourea, N-phenylthiourea, dithiocarbamate, and cyanide, but show different pH behavior using catechol as substrate. Atomic absorption spectrosopic analysis found 1.5 copper atoms per protein molecule. Using EPR spectroscopy we determined 1.8 Cu per molecule catechol oxidase. Furthermore, EPR spectroscopy demonstrated that catechol oxidase is a copper enzyme of type 3. The lack of an EPR signal is due to strong antiferromagnetic coupling that requires a bridging ligand between the two copper ions in the met preparation. Addition to H2O2 to both enzymes leads to oxy catechol oxidase. In the UV/Vis spectrum two new absorption bands occur at 345 nm and 580 nm. In accordance with the oxy forms of hemocyanin and tyrosinase the absorption band at 345 nm is due to an O2(2-) (pi sigma *)-->Cu(II) (dx2 - y2) charge transfer (CT) transition. The absorption band at 580 nm corresponds to the second O2(2)- (pi v*)-->Cu(II) (dx2 - y2) CT transition. The UV/Vis bands in combination with the resonance Raman spectra of oxy catechol oxidase indicate a mu-eta 2:eta 2 binding mode for dioxygen. The intense resonance Raman peak at 277 cm-1, belonging to a Cu-N (axial His) stretching mode, suggests that catechol oxidase has six terminal His ligands, as known for molluscan and arthropodan hemocyanin.
DOI: 10.1007/s007750050289
PubMed: 10499103
Affiliations:
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Rompel</name><affiliation wicri:level="1"><nlm:affiliation>Anorganisch-Chemisches Institut, Universität Münster, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Anorganisch-Chemisches Institut, Universität Münster</wicri:regionArea><wicri:noRegion>Universität Münster</wicri:noRegion><wicri:noRegion>Universität Münster</wicri:noRegion><wicri:noRegion>Universität Münster</wicri:noRegion></affiliation></author><author><name sortKey="Fischer, H" sort="Fischer, H" uniqKey="Fischer H" first="H" last="Fischer">H. Fischer</name></author><author><name sortKey="Meiwes, D" sort="Meiwes, D" uniqKey="Meiwes D" first="D" last="Meiwes">D. Meiwes</name></author><author><name sortKey="Buldt Karentzopoulos, K" sort="Buldt Karentzopoulos, K" uniqKey="Buldt Karentzopoulos K" first="K" last="Büldt-Karentzopoulos">K. Büldt-Karentzopoulos</name></author><author><name sortKey="Dillinger, R" sort="Dillinger, R" uniqKey="Dillinger R" first="R" last="Dillinger">R. Dillinger</name></author><author><name sortKey="Tuczek, F" sort="Tuczek, F" uniqKey="Tuczek F" first="F" last="Tuczek">F. Tuczek</name></author><author><name sortKey="Witzel, H" sort="Witzel, H" uniqKey="Witzel H" first="H" last="Witzel">H. Witzel</name></author><author><name sortKey="Krebs, B" sort="Krebs, B" uniqKey="Krebs B" first="B" last="Krebs">B. Krebs</name></author></analytic><series><title level="j">Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry</title><idno type="ISSN">0949-8257</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term><term>Catechol Oxidase (chemistry)</term><term>Catechol Oxidase (isolation & purification)</term><term>Catechol Oxidase (metabolism)</term><term>Catechols (metabolism)</term><term>Copper (metabolism)</term><term>Cyanides (pharmacology)</term><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Hemocyanins (chemistry)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Molecular Weight (MeSH)</term><term>Monophenol Monooxygenase (chemistry)</term><term>Phenylthiourea (pharmacology)</term><term>Plants (enzymology)</term><term>Spectrophotometry, Atomic (MeSH)</term><term>Spectrophotometry, Ultraviolet (MeSH)</term><term>Spectrum Analysis, Raman (MeSH)</term><term>Trees (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse spectrale Raman (MeSH)</term><term>Antienzymes (pharmacologie)</term><term>Arbres (enzymologie)</term><term>Catechol oxidase (composition chimique)</term><term>Catechol oxidase (isolement et purification)</term><term>Catechol oxidase (métabolisme)</term><term>Catéchols (métabolisme)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Cuivre (métabolisme)</term><term>Cyanures (pharmacologie)</term><term>Hémocyanine (composition chimique)</term><term>Masse moléculaire (MeSH)</term><term>Monophenol monooxygenase (composition chimique)</term><term>Phényl-thiourée (pharmacologie)</term><term>Plantes (enzymologie)</term><term>Sites de fixation (MeSH)</term><term>Spectrophotométrie UV (MeSH)</term><term>Spectrophotométrie atomique (MeSH)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Catechol Oxidase</term><term>Hemocyanins</term><term>Monophenol Monooxygenase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Catechol Oxidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Catechol Oxidase</term><term>Catechols</term><term>Copper</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cyanides</term><term>Enzyme Inhibitors</term><term>Phenylthiourea</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Catechol oxidase</term><term>Hémocyanine</term><term>Monophenol monooxygenase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arbres</term><term>Plantes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plants</term><term>Trees</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Catechol oxidase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Catechol oxidase</term><term>Catéchols</term><term>Cuivre</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antienzymes</term><term>Cyanures</term><term>Phényl-thiourée</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Electron Spin Resonance Spectroscopy</term><term>Hydrogen-Ion Concentration</term><term>Molecular Weight</term><term>Spectrophotometry, Atomic</term><term>Spectrophotometry, Ultraviolet</term><term>Spectrum Analysis, Raman</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse spectrale Raman</term><term>Concentration en ions d'hydrogène</term><term>Masse moléculaire</term><term>Sites de fixation</term><term>Spectrophotométrie UV</term><term>Spectrophotométrie atomique</term><term>Spectroscopie de résonance de spin électronique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We purified two catechol oxidases from Lycopus europaeus and Populus nigra which only catalyze the oxidation of catechols to quinones without hydroxylating tyrosine. The molecular mass of the Lycopus enzyme was determined to 39,800 Da and the mass of the Populus enzyme was determined to 56,050 Da. Both catechol oxidases are inhibited by thiourea, N-phenylthiourea, dithiocarbamate, and cyanide, but show different pH behavior using catechol as substrate. Atomic absorption spectrosopic analysis found 1.5 copper atoms per protein molecule. Using EPR spectroscopy we determined 1.8 Cu per molecule catechol oxidase. Furthermore, EPR spectroscopy demonstrated that catechol oxidase is a copper enzyme of type 3. The lack of an EPR signal is due to strong antiferromagnetic coupling that requires a bridging ligand between the two copper ions in the met preparation. Addition to H2O2 to both enzymes leads to oxy catechol oxidase. In the UV/Vis spectrum two new absorption bands occur at 345 nm and 580 nm. In accordance with the oxy forms of hemocyanin and tyrosinase the absorption band at 345 nm is due to an O2(2-) (pi sigma *)-->Cu(II) (dx2 - y2) charge transfer (CT) transition. The absorption band at 580 nm corresponds to the second O2(2)- (pi v*)-->Cu(II) (dx2 - y2) CT transition. The UV/Vis bands in combination with the resonance Raman spectra of oxy catechol oxidase indicate a mu-eta 2:eta 2 binding mode for dioxygen. The intense resonance Raman peak at 277 cm-1, belonging to a Cu-N (axial His) stretching mode, suggests that catechol oxidase has six terminal His ligands, as known for molluscan and arthropodan hemocyanin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10499103</PMID><DateCompleted><Year>1999</Year><Month>10</Month><Day>28</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>03</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0949-8257</ISSN><JournalIssue CitedMedium="Print"><Volume>4</Volume><Issue>1</Issue><PubDate><Year>1999</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry</Title><ISOAbbreviation>J Biol Inorg Chem</ISOAbbreviation></Journal><ArticleTitle>Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: evidence for a dinuclear copper center of type 3 and spectroscopic similarities to tyrosinase and hemocyanin.</ArticleTitle><Pagination><MedlinePgn>56-63</MedlinePgn></Pagination><Abstract><AbstractText>We purified two catechol oxidases from Lycopus europaeus and Populus nigra which only catalyze the oxidation of catechols to quinones without hydroxylating tyrosine. The molecular mass of the Lycopus enzyme was determined to 39,800 Da and the mass of the Populus enzyme was determined to 56,050 Da. Both catechol oxidases are inhibited by thiourea, N-phenylthiourea, dithiocarbamate, and cyanide, but show different pH behavior using catechol as substrate. Atomic absorption spectrosopic analysis found 1.5 copper atoms per protein molecule. Using EPR spectroscopy we determined 1.8 Cu per molecule catechol oxidase. Furthermore, EPR spectroscopy demonstrated that catechol oxidase is a copper enzyme of type 3. The lack of an EPR signal is due to strong antiferromagnetic coupling that requires a bridging ligand between the two copper ions in the met preparation. Addition to H2O2 to both enzymes leads to oxy catechol oxidase. In the UV/Vis spectrum two new absorption bands occur at 345 nm and 580 nm. In accordance with the oxy forms of hemocyanin and tyrosinase the absorption band at 345 nm is due to an O2(2-) (pi sigma *)-->Cu(II) (dx2 - y2) charge transfer (CT) transition. The absorption band at 580 nm corresponds to the second O2(2)- (pi v*)-->Cu(II) (dx2 - y2) CT transition. The UV/Vis bands in combination with the resonance Raman spectra of oxy catechol oxidase indicate a mu-eta 2:eta 2 binding mode for dioxygen. The intense resonance Raman peak at 277 cm-1, belonging to a Cu-N (axial His) stretching mode, suggests that catechol oxidase has six terminal His ligands, as known for molluscan and arthropodan hemocyanin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rompel</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Anorganisch-Chemisches Institut, Universität Münster, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fischer</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Meiwes</LastName><ForeName>D</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Büldt-Karentzopoulos</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Dillinger</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Tuczek</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Witzel</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Krebs</LastName><ForeName>B</ForeName><Initials>B</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>J Biol Inorg Chem</MedlineTA><NlmUniqueID>9616326</NlmUniqueID><ISSNLinking>0949-8257</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002396">Catechols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003486">Cyanides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>6F82C6Q54C</RegistryNumber><NameOfSubstance UI="D010670">Phenylthiourea</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>9013-72-3</RegistryNumber><NameOfSubstance UI="D006433">Hemocyanins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.1</RegistryNumber><NameOfSubstance UI="D004156">Catechol Oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.18.1</RegistryNumber><NameOfSubstance UI="D014442">Monophenol Monooxygenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>LF3AJ089DQ</RegistryNumber><NameOfSubstance UI="C034221">catechol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004156" MajorTopicYN="N">Catechol Oxidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002396" MajorTopicYN="N">Catechols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003486" MajorTopicYN="N">Cyanides</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006433" MajorTopicYN="N">Hemocyanins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014442" MajorTopicYN="N">Monophenol Monooxygenase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010670" MajorTopicYN="N">Phenylthiourea</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013054" MajorTopicYN="N">Spectrophotometry, Atomic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013056" MajorTopicYN="N">Spectrophotometry, Ultraviolet</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013059" MajorTopicYN="N">Spectrum Analysis, Raman</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>9</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>9</Month><Day>28</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>9</Month><Day>28</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10499103</ArticleId><ArticleId IdType="doi">10.1007/s007750050289</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Buldt Karentzopoulos, K" sort="Buldt Karentzopoulos, K" uniqKey="Buldt Karentzopoulos K" first="K" last="Büldt-Karentzopoulos">K. Büldt-Karentzopoulos</name><name sortKey="Dillinger, R" sort="Dillinger, R" uniqKey="Dillinger R" first="R" last="Dillinger">R. Dillinger</name><name sortKey="Fischer, H" sort="Fischer, H" uniqKey="Fischer H" first="H" last="Fischer">H. Fischer</name><name sortKey="Krebs, B" sort="Krebs, B" uniqKey="Krebs B" first="B" last="Krebs">B. Krebs</name><name sortKey="Meiwes, D" sort="Meiwes, D" uniqKey="Meiwes D" first="D" last="Meiwes">D. Meiwes</name><name sortKey="Tuczek, F" sort="Tuczek, F" uniqKey="Tuczek F" first="F" last="Tuczek">F. Tuczek</name><name sortKey="Witzel, H" sort="Witzel, H" uniqKey="Witzel H" first="H" last="Witzel">H. Witzel</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Rompel, A" sort="Rompel, A" uniqKey="Rompel A" first="A" last="Rompel">A. Rompel</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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