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Coupling of native IEF and extended X-ray absorption fine structure to characterize zinc-binding sites from pI isoforms of SOD1 and A4V pathogenic mutant

dc.contributor.authorCHEVREUX, S.
hal.structure.identifierService de Physique des Matériaux et Microstructures [SP2M - UMR 9002]
dc.contributor.authorLLORENS, I.
dc.contributor.authorLORENZO SOLARI, P.
hal.structure.identifierInterface Physique et Chimie pour le Vivant [IPCV]
dc.contributor.authorROUDEAU, S.
hal.structure.identifierInterface Physique et Chimie pour le Vivant [IPCV]
dc.contributor.authorDEVÈS, Guillaume
hal.structure.identifierInterface Physique et Chimie pour le Vivant [IPCV]
dc.contributor.authorCARMONA, A.
hal.structure.identifierMatériaux, Rayonnements, Structure [NEEL - MRS]
dc.contributor.authorTESTEMALE, Denis
hal.structure.identifierMatériaux, Rayonnements, Structure [NEEL - MRS]
dc.contributor.authorHAZEMANN, Jean-Louis
hal.structure.identifierInterface Physique et Chimie pour le Vivant [IPCV]
dc.contributor.authorORTEGA, R.
dc.date.issued2012
dc.identifier.issn0173-0835
dc.description.abstractEnExtended X-ray absorption fine structure (EXAFS) has already provided high-resolution structures of metal-binding sites in a wide variety of metalloproteins. Usually, EXAFS is performed on purified metalloproteins either in solution or crystallized form but purification steps are prone tomodify the metallation state of the protein. We developed a protocol to couple EXAFS analysis to metalloprotein separation using native gel electrophoresis. This coupling opens a large field of applications as metalloproteins can be characterized in their native state avoiding purification steps. Using native isoelectric focusing, the method enables the EXAFS analysis of metalloprotein pI isoforms. We applied this methodology to SOD1, wild-type, and Ala4Val mutant (A4V), a mutation found in amyotrophic lateral sclerosis (ALS) because decreased Zn affinity to SOD1 mutants is suggested to be involved in the pathogenesis of this neurodegenerative disease. We observed similar coordination structures for Zn in wild-type and mutant proteins, in all measured pI isoforms, demonstrating the feasibility of EXAFS on electrophoresis gels and suggesting that the Zn-binding site is not structurally modified in A4V SOD1 mutant
dc.language.isoen
dc.publisherWiley-VCH Verlag
dc.title.enCoupling of native IEF and extended X-ray absorption fine structure to characterize zinc-binding sites from pI isoforms of SOD1 and A4V pathogenic mutant
dc.typeArticle de revue
dc.identifier.doi10.1002/elps.201100596
dc.subject.halChimie/Chimie analytique
bordeaux.journalElectrophoresis
bordeaux.page1276-1281
bordeaux.volume33
bordeaux.peerReviewedoui
hal.identifierin2p3-00699389
hal.version1
hal.popularnon
hal.audienceNon spécifiée
dc.subject.esNative IEF
dc.subject.esSuperoxide dismutase 1
dc.subject.esX-ray Absorption Spectroscopy
dc.subject.esZinc
hal.origin.linkhttps://hal.archives-ouvertes.fr//in2p3-00699389v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Electrophoresis&rft.date=2012&rft.volume=33&rft.spage=1276-1281&rft.epage=1276-1281&rft.eissn=0173-0835&rft.issn=0173-0835&rft.au=CHEVREUX,%20S.&LLORENS,%20I.&LORENZO%20SOLARI,%20P.&ROUDEAU,%20S.&DEV%C3%88S,%20Guillaume&rft.genre=article


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