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dc.contributor.authorRoss, Teresa Adrianna Coleman
dc.date.accessioned2014-03-04T02:52:20Z
dc.date.available2014-03-04T02:52:20Z
dc.date.issued2007-12
dc.identifier.otherross_teresa_a_200712_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/ross_teresa_a_200712_ms
dc.identifier.urihttp://hdl.handle.net/10724/24481
dc.description.abstractFerrochelatase is the terminal enzyme in the heme biosynthetic pathway and catalyzes the insertion of ferrous iron into protoporphyrin IX in the formation of protoheme IX. Little is known about how substrate iron is acquired and taken up by the enzyme or how the enzyme functions at the cellular level. Here we investigated the putative roles of several amino acid residues in vivo by constructing and analyzing site-directed mutants within the C-terminus, on the protein surface, and inside the active site of human ferrochelatase. In vivo function of the enzyme was assessed by monitoring complementation, cellular growth rates and heme production in a ferrochelatase-deficient strain of Saccharomyces cerevisiae. The data suggest a possible surface site that may be involved in ferrochelatase function. These initial in vivo characterizations may lead to future advances in identifying specific amino acid residues that play a role in ferrochelatase function.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectFerrochelatase
dc.subjectS. cerevisiae
dc.subjectin vivo
dc.titleIn vivo analysis of wild-type and variant human ferrochelatases
dc.typeThesis
dc.description.degreeMS
dc.description.departmentBiochemistry and Molecular Biology
dc.description.majorBiochemistry and Molecular Biology
dc.description.advisorHarry A. Dailey
dc.description.committeeHarry A. Dailey
dc.description.committeeAlan Przybyla
dc.description.committeeClaiborne Glover, III


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