Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/6638
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dc.contributor.authorPinakoulaki, Eftychiaen
dc.contributor.authorPavlou, Andreaen
dc.contributor.authorKoutsoupakis, Constantinos-
dc.contributor.otherΚουτσουπάκης, Κωνσταντίνος-
dc.date.accessioned2013-01-21T13:41:59Zen
dc.date.accessioned2013-05-16T06:25:14Z-
dc.date.accessioned2015-12-02T09:54:04Z-
dc.date.available2013-01-21T13:41:59Zen
dc.date.available2013-05-16T06:25:14Z-
dc.date.available2015-12-02T09:54:04Z-
dc.date.issued2011en
dc.identifier.citationJournal of Physical Chemistry B, 2011, Volume 115, Issue 44, Pages 13012-13018en
dc.identifier.issn15206106en
dc.identifier.urihttp://ktisis.cut.ac.cy/handle/10488/6638en
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 H 2O/D 2O 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.; et 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 TRS 2-FTIR spectra show that the rate of recombination of CO to the heme is k 1945 cm -1 = 126 ± 20 s -1 and k 1964 cm -1 = 122 ± 20 s -1 at pH 5.6, and k 1945 cm -1 = 148 ± 30 s -1 and k 1964 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.en
dc.formatpdfen
dc.language.isoenen
dc.publisherAmerican Chemical Society Publicationsen
dc.rights© 2011 American Chemical Society.en
dc.subjectCyanidesen
dc.subjectPorphyrinsen
dc.subjectCarbon monoxideen
dc.subjectNitrogenen
dc.titleAldoxime dehydratase: probing the heme environment involved in the synthesis of the carbon-nitrogen triple bonden
dc.typeArticleen
dc.affiliationUniversity of Cyprusen
dc.identifier.doi10.1021/jp205944een
dc.dept.handle123456789/54en
item.grantfulltextnone-
item.fulltextNo Fulltext-
item.languageiso639-1other-
crisitem.author.deptDepartment of Environmental Science and Technology-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.orcid0000-0001-9301-1021-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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