Photoelectroenzymatic Oxyfunctionalization on Flavin-Hybridized Carbon Nanotube Electrode Platform

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dc.contributor.authorChoi, Da Somko
dc.contributor.authorNi, Yanko
dc.contributor.authorFernandez-Fueyo, Elenako
dc.contributor.authorLee, Minahko
dc.contributor.authorHollmann, Frankko
dc.contributor.authorPark, Chan Beumko
dc.date.accessioned2017-04-17T07:26:28Z-
dc.date.available2017-04-17T07:26:28Z-
dc.date.created2017-04-10-
dc.date.created2017-04-10-
dc.date.issued2017-03-
dc.identifier.citationACS CATALYSIS, v.7, no.3, pp.1563 - 1567-
dc.identifier.issn2155-5435-
dc.identifier.urihttp://hdl.handle.net/10203/223234-
dc.description.abstractPeroxygenases are very promising catalysts for oxyfunctionalization reactions. Their practical applicability, H2O2 however, is hampered by their sensitivity against the oxidant (H2O2), therefore necessitating in situ generation of H2O2. Here, we report a photoelectrochemical approach to provide peroxygenases with suitable amounts of H2O2 while reducing the electrochemical overpotential needed for the reduction of molecular oxygen to H2O2. When tethered on single-walled carbon nanotubes (SWNTs) under illumination, flavins allowed for a marked anodic shift of the oxygen reduction potential in comparison to pristine SWNT and/or non illuminated electrodes. This flavin-SWNT-based photoelectrochemical platform enabled peroxygenases-catalyzed, selective hydroxylation reactions.-
dc.languageEnglish-
dc.publisherAMER CHEMICAL SOC-
dc.subjectCATALYZED OXYFUNCTIONALIZATION-
dc.subjectELECTROCHEMICAL GENERATION-
dc.subjectUNSPECIFIC PEROXYGENASE-
dc.subjectBIENZYMATIC SYSTEM-
dc.subjectOXIDATION-
dc.subjectCHLOROPEROXIDASE-
dc.subjectPEROXIDASE-
dc.subjectH2O2-
dc.subjectMONONUCLEOTIDE-
dc.subjectOXIDASE-
dc.titlePhotoelectroenzymatic Oxyfunctionalization on Flavin-Hybridized Carbon Nanotube Electrode Platform-
dc.typeArticle-
dc.identifier.wosid000395726500006-
dc.identifier.scopusid2-s2.0-85021676808-
dc.type.rimsART-
dc.citation.volume7-
dc.citation.issue3-
dc.citation.beginningpage1563-
dc.citation.endingpage1567-
dc.citation.publicationnameACS CATALYSIS-
dc.identifier.doi10.1021/acscatal.6b03453-
dc.contributor.localauthorPark, Chan Beum-
dc.contributor.nonIdAuthorNi, Yan-
dc.contributor.nonIdAuthorFernandez-Fueyo, Elena-
dc.contributor.nonIdAuthorHollmann, Frank-
dc.description.isOpenAccessN-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorheme proteins-
dc.subject.keywordAuthoroxyfunctionalization-
dc.subject.keywordAuthorphotoelectrochemistry-
dc.subject.keywordAuthorflavins-
dc.subject.keywordAuthorperoxygenases-
dc.subject.keywordPlusCATALYZED OXYFUNCTIONALIZATION-
dc.subject.keywordPlusELECTROCHEMICAL GENERATION-
dc.subject.keywordPlusUNSPECIFIC PEROXYGENASE-
dc.subject.keywordPlusBIENZYMATIC SYSTEM-
dc.subject.keywordPlusOXIDATION-
dc.subject.keywordPlusCHLOROPEROXIDASE-
dc.subject.keywordPlusPEROXIDASE-
dc.subject.keywordPlusH2O2-
dc.subject.keywordPlusMONONUCLEOTIDE-
dc.subject.keywordPlusOXIDASE-
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