A study on a primitive artificial esterase model: Reactivity of a calix[4]resorcinarene bearing carboxyl groups

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dc.contributor.authorCevasco, Giorgio
dc.contributor.authorGalatini, Andrea
dc.contributor.authorPirinççioğlu, Necmettin
dc.contributor.authorThea, Sergio
dc.contributor.authorWilliams, Andrew
dc.contributor.orcid0000-0001-9805-9745
dc.date.accessioned2024-04-24T17:56:02Z
dc.date.available2024-04-24T17:56:02Z
dc.date.issued2008
dc.departmentDicle Üniversitesi, Fen Fakültesi, Kimya Bölümüen_US
dc.description.abstractThe host molecule octacarboxymethyl calix[4]resorcinarene 1 catalyses the hydrolysis of substituted phenyl N-methylpyridinium-4-carboxylate esters 3a-f by complexation followed by intracomplex reaction via an anhydride intermediate. The reactivity in the presence of 1 is higher than that of the background at low pH; at high pH an inversion of reactivity occurs, the background becomes predominant since the host inhibits hydrolysis of the esters. The reactivity of esters 3a-f complexed with the host suffers little change in effective charge on the phenolic oxygen (-0.15 units) in contrast with the changes observed in alkaline hydrolysis (-0.28 units) and in the hydrolysis of the model monoaryl glutarate esters (-1.02 units). The less negative effective charge in the transition state for host 1 catalysis compared with that in the glutarate case is ascribed to stronger solvation by water molecules in the complex compared with that due to water molecules in the bulk solvent.en_US
dc.identifier.citationCevasco, G., Galatini, A., Pirinççioğlu, N., Thea, S. ve Williams, A. (2008). A study on a primitive artificial esterase model: Reactivity of a calix[4]resorcinarene bearing carboxyl groups. Journal of Physical Organic Chemistry, 21(6), 498-504.
dc.identifier.doi10.1002/poc.1371
dc.identifier.endpage504en_US
dc.identifier.issn0894-3230
dc.identifier.issue6en_US
dc.identifier.scopus2-s2.0-46649091126
dc.identifier.scopusqualityQ3
dc.identifier.startpage498en_US
dc.identifier.urihttps://doi.org/10.1002/poc.1371
dc.identifier.urihttps://hdl.handle.net/11468/23200
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/10.1002/poc.1371
dc.identifier.volume21en_US
dc.indekslendigikaynakScopus
dc.language.isoenen_US
dc.relation.ispartofJournal of Physical Organic Chemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCalixresorcinarenesen_US
dc.subjectCatalysisen_US
dc.subjectEster hydrolysisen_US
dc.subjectMolecular receptorsen_US
dc.titleA study on a primitive artificial esterase model: Reactivity of a calix[4]resorcinarene bearing carboxyl groupsen_US
dc.titleA study on a primitive artificial esterase model: Reactivity of a calix[4]resorcinarene bearing carboxyl groups
dc.typeArticleen_US

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