Biomedical application of M？ssbauer spectroscopy with a high velocity resolution Revealing of small variations英文文献资料.docVIP

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Biomedical application of M？ssbauer spectroscopy with a high velocity resolution Revealing of small variations英文文献资料.doc

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Biomedical application of M？ssbauer spectroscopy with a high velocity resolution Revealing of small variations英文文献资料

Spectroscopy24(2010)593–599 DOI10.3233/SPE-2010-0489 IOSPress 593 BiomedicalapplicationofM?ssbauer spectroscopywithahighvelocityresolution: Revealingofsmallvariations M.I.Oshtrakha,?,V.A.Semionkin ,O.B.Milder ,I.V.Alenkina andE.G.Novikov a,b a,c a,b a,b aFacultyofPhysicalTechniquesandDevicesforQualityControl,Physical–TechnicalDepartment, UralFederalUniversity,Ekaterinburg,RussianFederation bFacultyofExperimentalPhysics,Physical–TechnicalDepartment,UralFederalUniversity, Ekaterinburg,RussianFederation cRadio–TechnicalDepartment,UralFederalUniversity,Ekaterinburg,RussianFederation Abstract.Application ofM?ssbauerspectroscopywith ahighvelocity resolution forstudydifferent hemoglobins, ferritin, its models and chicken liver and spleen as well as normal and lymphoid chicken spleen demonstrated revealing of small variationsofhyper?neparametersrelatedtosmallvariationsofironstereochemistryinbiomolecules.Thesedatademonstrate thatM?ssbauerspectroscopywithahighvelocityresolutionmaybeusefulinbiomedicalresearchtodistinguishsmallvariations ofiron-containingproteinsinnormalandpathologicalcases. Keywords:M?ssbauerspectroscopywithahighvelocityresolution,biomedicalapplications,smallvariations 1. Introduction M?ssbauerspectroscopyisapowerfultoolwhichallowsustoobservethehyper?nesplittingofthe nuclearenergylevelsaswellaschangesofenergiesofthegroundandexcitedstatesofM?ssbauernuclei (forinstance, 57Fe, 119Sn, 197Auandsomeother)intheabsorptionoremissionspectrumofγ-rays(de- taileddescriptionoftheM?ssbauereffectsee,forinstance,in[1–3,16]).Ironisoneofthemostvitally importantmetals.Anumberofproteinscontainironasanactivesite.Someproteinsareresponsiblefor theirontransportandstorage.Thefunctionalpropertiesoftheseproteinsaredeterminedinpartbythe ironelectronicstructureandstereochemistry.Therefore,somefunctionalvariationsofproteinsrelated tothestructuralheterogeneitymaybere?ectedbythesmallchangesoftheironelectronicstructure. Itiswellknownthatsevera