CHED 1226 |
| Catalase-peroxidase (KatG) from Mycobacterium tuberculosis (Mtb) is a bifunctional oxidoreductase that activates isoniazid (INH), a pro-drug that is a frontline antibiotic used in the treatment of TB. An attractive method to probe the reactivity of this hemoprotein is through the use of cavity mutants, such as KatG(H270G), that allow for small molecules to bind to the heme center in the proximal position. Preliminary UV-Visible spectroscopic studies suggest a change in the electronic state of the heme upon binding of several exogenous N and O donor ligands, including imidazole, pyridine, and furan. Peroxidase and catalase activity measurements with these ligands will be correlated with their electronic properties. Details from Resonance Raman spectroscopy pertaining to spin state and ligand binding efficiency will also be presented. |
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Undergraduate Research Poster Session: Inorganic Chemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |