1. Repository of OAI
  2. ΑΠΟΘΕΤΗΡΙΟ "ΟΛΥΜΠΙΑΣ"
  3. Σχολή Θετικών Επιστημών
  4. Τμήμα Χημείας
  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
Ελληνικά   English  
Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/9851
Full metadata record
DC FieldValueLanguage
dc.contributor.authorLazarides, T.en
dc.contributor.authorSazanovich, I. V.en
dc.contributor.authorSimaan, A. J.en
dc.contributor.authorKafentzi, M. C.en
dc.contributor.authorDelor, M.en
dc.contributor.authorMekmouche, Y.en
dc.contributor.authorFaure, B.en
dc.contributor.authorReglier, M.en
dc.contributor.authorWeinstein, J. A.en
dc.contributor.authorCoutsolelos, A. G.en
dc.contributor.authorTron, T.en
dc.date.accessioned2015-11-24T16:52:13Z-
dc.date.available2015-11-24T16:52:13Z-
dc.identifier.issn0002-7863-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9851-
dc.rightsDefault Licence-
dc.subjectintramolecular electron-transferen
dc.subjectblue copper proteinsen
dc.subjectwater-soluble porphyrinsen
dc.subjectlaser flash-photolysisen
dc.subjectcytochrome-cen
dc.subjectascorbate oxidaseen
dc.subjectphotocatalytic oxidationen
dc.subjectmulticopper oxidasesen
dc.subjectpulse-radiolysisen
dc.subjectaqueous-solutionen
dc.titleVisible Light-Driven O-2 Reduction by a Porphyrin-Laccase Systemen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1021/Ja309969s-
heal.identifier.secondary<Go to ISI>://000315618900042-
heal.identifier.secondaryhttp://pubs.acs.org/doi/pdfplus/10.1021/ja309969s-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2013-
heal.abstractSeveral recent studies have shown that the combination of photosensitizers with metalloenzymes can support a light-driven multielectron reduction of molecules such as CO2 or HCN. Here we show that the association of the zinc tetramethylpyridinium porphyrin (ZnTMPyP4+) photosensitizer with the multicopper oxidase (MCO) laccase allows to link the oxidation of an organic molecule to the four electrons reduction of dioxygen into water. The enzyme is photoreduced within minutes with porphyrin/enzyme ratio as low as 1:40. With a 1:1 ratio, the dioxygen consumption rate is 1.7 mu mol L-1 s(-1). Flash photolysis experiments support the formation of the triplet excited state of ZnTMPyP4+ which reduces the enzyme to form a radical cation of the porphyrin with a k(ET) approximate to 10(7) s(-1) M-1. The long-lived triplet excited state of the ZnTMPyP4+ (tau(0) = 0.72 ms) accounts for a substantial electron-transfer quantum yield, phi(ET) = 0.35. Consequently, the enzyme-dependent photo-oxidation of the electron donor occurs with a turnover of 8 min(-1) for the one-electron oxidation process, thereby supporting the suitability of such enzyme/sensitizer hybrid systems for aerobic photodriven transformations on substrates. This study is the first example of a phorphyrin-sensitized four-electron reduction of an enzyme of the MCO family, leading to photoreduction of dioxygen into water.en
heal.publisherAmerican Chemical Societyen
heal.journalNameJ Am Chem Socen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

Show simple item record
Files in This Item:
File Description SizeFormat 
Lazarides-2013-Visible Light-Driven.pdf436.39 kBAdobe PDFView/Open    Request a copy
Show simple item record  


This item is licensed under a Creative Commons License Creative Commons