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dc.contributor.authorCheatum, Wren Hilliard
dc.date.accessioned2014-03-04T18:18:28Z
dc.date.available2014-03-04T18:18:28Z
dc.date.issued2009-08
dc.identifier.othercheatum_wren_h_200908_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/cheatum_wren_h_200908_ms
dc.identifier.urihttp://hdl.handle.net/10724/25764
dc.description.abstractReactive oxygen species, such as superoxide, are associated with many diseases including cancer, diabetes, and atherosclerosis. In order to protect against the presence of reactive oxygen species, organisms have evolved mechanisms to detoxify superoxide mediated by the enzymes superoxide dismutase (SOD) and superoxide reductase (SOR). SOR is a non-heme iron enzyme present in anaerobic and microaerophilic biological systems that is utilized for the detoxification of superoxide via its one-electron reduction to form hydrogen peroxide. The present work describes the synthetic analogs of the active site of SOR through the utilization of neutral, nitrogenous ligands in combination with exogenous thiolate ligands about an iron center in order to mimic the histidine and cysteine residues of the enzyme. The varying nitrogenous ligands include pyridine and imidazole substituents as the nitrogen donor. The synthesis and characterization of theses model systems contributes to the understanding of the mechanism of SOR.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectSuperoxide
dc.subjectSuperoxide reductase
dc.subjectNon-heme iron
dc.subjectBioinorganic chemistry
dc.subjectsynthetic analog
dc.titleSynthetic analogs of the non-heme iron center in superoxide reductase
dc.typeThesis
dc.description.degreeMS
dc.description.departmentChemistry
dc.description.majorChemistry
dc.description.advisorTodd C. Harrop
dc.description.committeeTodd C. Harrop
dc.description.committeeMichael K. Johnson
dc.description.committeeMichael W.w. Adams


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