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dc.contributor.authorSağ Erdem, Safiye
dc.contributor.authorKarahan, Özlem
dc.contributor.authorYıldız, İbrahim
dc.contributor.authorYelekçi, Kemal
dc.date.accessioned2019-06-27T08:06:52Z
dc.date.available2019-06-27T08:06:52Z
dc.date.issued2006
dc.identifier.issn1477-0520
dc.identifier.issn1477-0539
dc.identifier.urihttps://hdl.handle.net/20.500.12469/1237
dc.identifier.urihttps://dx.doi.org/10.1039/b511350d
dc.description.abstractThe proposed polar nucleophilic mechanism of MAO was investigated using quantum chemical calculations employing the semi-empirical PM3 method. In order to mimic the reaction at the enzyme's active site the reactions between the flavin and the p-substituted benzylamine substrate analogs were modeled. Activation energies and rate constants of all the reactions were calculated and compared with the published experimental data. The results showed that electron-withdrawing groups at the para position of benzylamine increase the reaction rate. A good correlation between the log of the calculated rate constants and the electronic parameter (sigma) of the substituent was obtained. These results agree with the previous kinetic experiments on the effect of p-substituents on the reduction of MAO-A by benzylamine analogs. In addition the calculated rate constants showed a correlation with the rate of reduction of the flavin in MAO-A. In order to verify the results obtained from the PM3 method single-point B3LYP/6-31G*//PM3 calculations were performed. These results demonstrated a strong reduction in the activation energy for the reaction of benzylamine derivatives having electron-withdrawing substituents which is in agreement with the PM3 calculations and the previous experimental QSAR study. PM3 and B3LYP/6-31G* energy surfaces were obtained for the overall reaction of benzylamine with flavin. Results suggest that PM3 is a reasonable method for studying this kind of reaction. These theoretical findings support the proposed polar nucleophilic mechanism for MAO-A.
dc.language.isoEnglish
dc.publisherRoyal Soc Chemistry
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.titleA computational study on the amine-oxidation mechanism of monoamine oxidase: Insight into the polar nucleophilic mechanism
dc.typeArticle
dc.identifier.startpage646
dc.identifier.endpage658
dc.relation.journalOrganic & Biomolecular Chemistry
dc.identifier.issue4
dc.identifier.volume4
dc.identifier.wosWOS:000235778600019
dc.identifier.doi10.1039/b511350d
dc.contributor.khasauthorYelekçi, Kemal


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