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dc.contributor.authorPinakoulaki, Eftychiaen
dc.contributor.authorKoutsoupakis, Constantinosen
dc.contributor.authorSawai, H.en
dc.contributor.authorPavlou, A.en
dc.contributor.authorKato, Y.en
dc.contributor.authorAsano, Y.en
dc.contributor.authorAono, S.en
dc.creatorPinakoulaki, Eftychiaen
dc.creatorKoutsoupakis, Constantinosen
dc.creatorSawai, H.en
dc.creatorPavlou, A.en
dc.creatorKato, Y.en
dc.creatorAsano, Y.en
dc.creatorAono, S.en
dc.date.accessioned2019-11-21T06:22:19Z
dc.date.available2019-11-21T06:22:19Z
dc.date.issued2011
dc.identifier.issn1520-6106
dc.identifier.urihttp://gnosis.library.ucy.ac.cy/handle/7/56027
dc.description.abstractFourier transform infrared (FTIR) spectra, "light" minus "dark" difference FTIR spectra, and time-resolved step-scan (TRS 2) FTIR spectra are reported for carbonmonoxy aldoxime dehydratase. Two C-O modes of heme at 1945 and 1964 cm-1 have been identified and remained unchanged in H2O/D2O exchange and in the pH 5.6-8.5 range, suggesting the presence of two conformations at the active site. The observed C-O frequencies are 5 and 16 cm-1 lower and higher, respectively, than that obtained previously (Oinuma, K.-I.en
dc.description.abstractet al. FEBS Lett.2004, 568, 44-48). We suggest that the strength of the Fe-His bond and the neutralization of the negatively charged propionate groups modulate the ν(Fe-CO)/ν(CO) back-bonding correlation. The "light" minus "dark" difference FTIR spectra indicate that the heme propionates are in both the protonated and deprotonated forms, and the photolyzed CO becomes trapped within a ligand docking site (ν(CO) = 2138 cm-1). The TRS2-FTIR spectra show that the rate of recombination of CO to the heme is k1945 cm-1 = 126 ± 20 s -1 and k1964 cm-1 = 122 ± 20 s -1 at pH 5.6, and k1945 cm-1 = 148 ± 30 s-1 and k1964 cm-1 = 158 ± 32 s -1 at pH 8.5. The rate of decay of the heme propionate vibrations is on a time scale coincident with the rate of rebinding, suggesting that there is a coupling between ligation dynamics in the distal heme environment and the environment sensed by the heme propionates. The implications of these results with respect to the proximal His-Fe heme environment including the propionates and the positively charged or proton-donating residues in the distal pocket which are crucial for the synthesis of nitriles are discussed. © 2011 American Chemical Society.en
dc.sourceJournal of Physical Chemistry Ben
dc.source.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-80455129765&doi=10.1021%2fjp205944e&partnerID=40&md5=6a74e830eb2b986a6758d0487d641eed
dc.subjectTime-scalesen
dc.subjectVibrations (mechanical)en
dc.subjectVolatile fatty acidsen
dc.subjectTime-resolveden
dc.subjectCyanidesen
dc.subjectFT-IR spectrumen
dc.subjectFourier transformsen
dc.subjectProtonateden
dc.subjectActive siteen
dc.subjectFourier transform infrareden
dc.subjectPorphyrinsen
dc.subjectAldoxime dehydrataseen
dc.subjectBack-bondingen
dc.subjectDeprotonated formen
dc.subjectDistal pocketen
dc.subjectHeme propionatesen
dc.subjectLigand dockingen
dc.subjectPositively chargeden
dc.subjectRate of recombinationen
dc.subjectTriple bondsen
dc.titleAldoxime dehydratase: Probing the heme environment involved in the synthesis of the carbon-nitrogen triple bonden
dc.typeinfo:eu-repo/semantics/article
dc.identifier.doi10.1021/jp205944e
dc.description.volume115
dc.description.issue44
dc.description.startingpage13012
dc.description.endingpage13018
dc.author.faculty002 Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences
dc.author.departmentΤμήμα Χημείας / Department of Chemistry
dc.type.uhtypeArticleen
dc.description.notes<p>Cited By :7</p>en
dc.source.abbreviationJ Phys Chem Ben
dc.contributor.orcidPinakoulaki, Eftychia [0000-0003-3320-6112]
dc.gnosis.orcid0000-0003-3320-6112


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