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dc.contributor.supervisor Loewen, Peter (Microbiology) en_US
dc.contributor.author Jha, Vikash Kumar
dc.date.accessioned 2011-09-02T14:33:15Z
dc.date.available 2011-09-02T14:33:15Z
dc.date.issued 2011-09-02
dc.identifier.uri http://hdl.handle.net/1993/4829
dc.description.abstract Catalase HPII of Escherichia coli is similar in sequence and structure to other catalases including the conservation of several residues on both the distal and proximal sides of the active center heme. The roles of many residues on the distal side of the heme have been well characterized. By contrast, very few residues on the proximal side of the heme or in the plane of the heme have been investigated. The primary goal of this thesis is to develop a better understanding of the role of the residues and structural features at the core of catalases and in the lateral access channel. The results demonstrate that a break in molecular symmetry does not have any functional significance. Replacing Ile274 with a Cys resulted in the heme being covalently linked to the protein through a Cys-vinyl bond which is hypersensitive to X-ray irradiation being largely degraded within seconds of exposure to the X-ray beam. en_US
dc.rights info:eu-repo/semantics/openAccess
dc.subject catalase KatE en_US
dc.subject X-ray irradiation en_US
dc.title Structural and functional characterization of catalase HPII of Escherichia coli en_US
dc.type info:eu-repo/semantics/doctoralThesis
dc.type doctoral thesis en_US
dc.degree.discipline Microbiology en_US
dc.contributor.examiningcommittee Dibrov, Pavel (Microbiology) Oresnik, Ivan (Microbiology) Stetefeld, Jorg (Chemistry) Jia, Zongchao (Biochemistry, Queens University) en_US
dc.degree.level Doctor of Philosophy (Ph.D.) en_US
dc.description.note October 2011 en_US


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