B3LYP Study on Reduction Mechanisms from to at the Catalytic Sites of Fully Reduced and Mixed-Valence Bovine Cytochrome Oxidases英文文献资料.docVIP

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B3LYP Study on Reduction Mechanisms from to at the Catalytic Sites of Fully Reduced and Mixed-Valence Bovine Cytochrome Oxidases英文文献资料.doc

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B3LYP Study on Reduction Mechanisms from to at the Catalytic Sites of Fully Reduced and Mixed-Valence Bovine Cytochrome Oxidases英文文献资料

HindawiPublishingCorporation BioinorganicChemistryandApplications Volume2010,ArticleID182804,18pages doi:10.1155/2010/182804 ResearchArticle B3LYPStudyonReductionMechanismsfromO2toH2 Oat theCatalyticSitesofFullyReducedandMixed-ValenceBovine CytochromecOxidases YasunoriYoshiokaandMasakiMitani ChemistryDepartmentforMaterials,GraduateSchoolofEngineering,MieUniversity,Kurima-machiya1577,Tsu, Mie514-8507,Japan CorrespondenceshouldbeaddressedtoYasunoriYoshioka,yyoshi@chem.mie-u.ac.jp Received4August2009;Revised27November2009;Accepted5January2010 AcademicEditor:KonstantinosTsipis Copyright?2010Y.YoshiokaandM.Mitani.ThisisanopenaccessarticledistributedundertheCreativeCommonsAttribution License,whichpermitsunrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalworkisproperly cited. Reduction mechanisms of oxygen molecule to water molecules in the fully reduced (FR) and mixed-valence (MV) bovine cytochromecoxidases(CcO)havebeensystematicallyexaminedbasedontheB3LYPcalculations.Thecatalyticcycleusingfour electronsandfourprotonshasbeenalsoshownconsistently.TheMVCcOcatalysesreductiontoproduceonewatermolecule, whiletheFRCcOcatalysestoproducetwowatermolecules.OnewatermoleculeisaddedintovacantspacebetweenHis240 andHis290inthecatalyticsite.ThiswatermoleculeconstructsthenetworkofhydrogenbondsofTyr244,farnesylethyl,and Thr316thatisaterminalresidueoftheK-pathway.Itplayscrucialrolesfortheprotontransfertothedioxygentoproducethe watermoleculesinbothMVandFRCcOs.Tyr244functionsasarelayoftheprotontransferfromtheK-pathwaytotheadded watermolecule,notasdonorsofaprotonandanelectrontothedioxygen.ThereductionmechanismsofMVandFRCcOs arestrictlydistinguished.IntheFRCcO,theCuatomattheCuB sitemaintainsthereducedstateCu(I)duringtheprocessof formationof?rstwatermoleculeandplaysanelectronstorage.Atthe?nalstageofformationof?rstwatermolecule,theCu(I) atomreleasesanelectrontoFe-O.Duringtheprocessofformationofsecondwatermolecule,theCuatommaintainstheoxidized stateCu(II).Incontrastw