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A computational study on the amine-oxidation mechanism of monoamine oxidase: Insight into the polar nucleophilic mechanism

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dc.contributor.authorERDEM, SAFİYE
dc.contributor.authorsErdem, SS; Karahan, O; Yildiz, I; Yelekci, K
dc.date.accessioned2022-03-12T17:20:51Z
dc.date.available2022-03-12T17:20:51Z
dc.date.issued2006
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.identifier.doi10.1039/b511350d
dc.identifier.eissn1477-0539
dc.identifier.issn1477-0520
dc.identifier.pubmed16467939
dc.identifier.urihttps://hdl.handle.net/11424/228284
dc.identifier.wosWOS:000235778600019
dc.language.isoeng
dc.publisherROYAL SOC CHEMISTRY
dc.relation.ispartofORGANIC & BIOMOLECULAR CHEMISTRY
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectAGENT MILACEMIDE 2-(N-PENTYLAMINO)ACETAMIDE
dc.subjectB-CATALYZED OXIDATION
dc.subjectBENZYLAMINE ANALOGS
dc.subjectSUBSTITUTED BENZYLAMINES
dc.subjectENZYME CATALYSIS
dc.subjectHYDRIDE TRANSFER
dc.subjectCHEMICAL-MODEL
dc.subjectINACTIVATION
dc.subjectINHIBITORS
dc.subjectDEHALOGENASE
dc.titleA computational study on the amine-oxidation mechanism of monoamine oxidase: Insight into the polar nucleophilic mechanism
dc.typearticle
dspace.entity.typePublication
local.avesis.idb77c9ccb-b5fe-4cb6-b234-ea5f6576819c
local.import.packageSS17
local.indexed.atWOS
local.indexed.atSCOPUS
local.indexed.atPUBMED
local.journal.numberofpages13
oaire.citation.endPage658
oaire.citation.issue4
oaire.citation.startPage646
oaire.citation.titleORGANIC & BIOMOLECULAR CHEMISTRY
oaire.citation.volume4
relation.isAuthorOfPublication99f2f09c-7e48-402f-9bb9-ccdd73c27ec2
relation.isAuthorOfPublication.latestForDiscovery99f2f09c-7e48-402f-9bb9-ccdd73c27ec2

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