Modeling of molecular interaction between catechol and tyrosinase by DFT

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dc.contributor.authorPolatoglu, I
dc.contributor.authorKaratas, D
dc.date.accessioned2024-07-18T11:51:14Z
dc.date.available2024-07-18T11:51:14Z
dc.description.abstractIn this study, the synthetic active site model of tyrosinase enzyme's (His(3))(CuOHCu)-O-center dot center dot-Cu-center dot center dot(His(3)) arrangement is constituted by applying the density functional theory (DFT) to reveal the enzymatic conversion of catechol in molecular basis. This is the first time the binding mechanisms of catechol in relation to the enzyme active site (met-tyrosinase) in a vacuum environment, explicit water, and solvent (ethanol, acetone)/water mixture have been studied using the DFT. The theoretical results are supported along with the experimental ones to clarify the structure-activity relationship in these models. As understood from the mechanisms, the initial H abstraction from catechol is the most probable rate-limiting step. The parameters that cause the copper region to become congested or comfortable for H abstraction, such as the ordered structure of water molecules, Cu-Cu distance, H-bond distance, orientation and conformation of histidine residues around the copper center, and electrostatic potential of the system, play a significant role in the catechol/met-tyrosinase interaction. (C) 2019 Elsevier B.V. All rights reserved.
dc.identifier.issn0022-2860
dc.identifier.other1872-8014
dc.identifier.urihttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/4705
dc.language.isoEnglish
dc.publisherELSEVIER
dc.subjectMUSHROOM TYROSINASE
dc.subjectACTIVE-SITE
dc.subjectCATALYTIC CYCLE
dc.subjectOXIDATION
dc.subjectINHIBITORS
dc.subjectCOMPLEXES
dc.subjectMONOOXYGENATION
dc.subjectACTIVATION
dc.subjectBIOSENSOR
dc.subjectMECHANISM
dc.titleModeling of molecular interaction between catechol and tyrosinase by DFT
dc.typeArticle

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