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dc.contributor.authorRandeniya, Sajini Ransara
dc.date.accessioned2014-03-04T20:59:54Z
dc.date.available2014-03-04T20:59:54Z
dc.date.issued2012-12
dc.identifier.otherrandeniya_sajini_r_201212_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/randeniya_sajini_r_201212_ms
dc.identifier.urihttp://hdl.handle.net/10724/28590
dc.description.abstractThe A-type proteins are a class of [Fe-S]-cluster biogenesis proteins which are found in all domains of life. However, the specific function(s) of these A-type proteins within the mitochondrial and bacterial Fe/S-protein biogenesis are still unknown. The ability of Azotobacter vinelandii(Av) IscA and Arabidopsis thaliana(At) SufA1 to bind Fe and [Fe-S]-cluster has been investigated to assess the potential role(s) of A-type proteins in [Fe-S]-cluster biogenesis. Both A-type proteins have been shown to bind one Fe(III) per homodimer with an intermediate-spin (S = 3/2) Fe(III) center that is most likely 5-coordinate with two or three cysteinate ligands. Further, AtSufA1 is shown to bind one [2Fe-2S]2+-cluster with complete cysteinyl ligation. In addition, in vitro UV-visible CD studies of rapid cluster transfer from AtGrxS14 to AtSufA1 yielding a rate constant of 50000 M-1min-1 and >95% completion within 3min indicate that these two classes of proteins work together in cellular [Fe-S]-cluster trafficking.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectIron-sulfur cluster assembly
dc.subjectA-type protein
dc.subjectMonothiol glutaredoxins
dc.subjectCluster transfer
dc.titleCharacterization of the roles of A-type proteins in iron-sulfur cluster biogenesis
dc.typeThesis
dc.description.degreeMS
dc.description.departmentChemistry
dc.description.majorChemistry
dc.description.advisorMichael K. Johnson
dc.description.committeeMichael K. Johnson
dc.description.committeeTodd C. Harrop
dc.description.committeeMichael W.w. Adams


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