Date of Thesis Acceptance
Major Department or Program
Biochemistry, Biophysics and Molecular Biology
The molybdenum-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans is a metalloenzyme that converts carbon monoxide and water to carbon dioxide, producing two protons and two electrons in the process. This enzyme is responsible for the removal approximately 200 million tons of toxic carbon monoxide from the atmosphere each year. Despite its importance to the global carbon cycle, the mechanism of the enzyme is still not well understood. Efforts have been made to create biomimetic compounds that would allow for investigation of the catalytic cycle, but results have only shown limited success, recreating geometric features but unable to perform catalysis.
We report here the design of a new biomimetic compound, based on a previous synthetic model reported by Gourlay et al., in order to investigate the catalytic cycle of carbon monoxide dehydrogenase. This design began with a computational investigation of several versions of the compounds with different ligands used to coordinate the molybdenum center. Geometry optimizations were performed and critical atom distances and angles were compared to those found in the experimental data for carbon monoxide dehydrogenase.
Based on these investigations, a ligand was chosen for the model complex and work began on synthesizing the desired final complex. Ligand synthesis and coordination of these ligands to the metal centers was performed. Though the final complex was not isolated, two novel metal-ligand complexes were isolated.
Carbon monoxide dehydrogenase -- Environmental aspects, Gram-negative aerobic bacteria -- Oliotropha carboxidovorans, Ligand binding (Biochemistry) -- Research-- Methodology, Aerobic bacteria, Whitman College 2016 -- Dissertation collection -- Biochemistry‚ Biophysics‚ and Molecular Biology
Whitman Community Accessible Thesis
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O'Connor, Jacob J., "Computational and Synthetic Design of Biomimetic Model Complexes of the Mo-Cu Carbon Monoxide Dehydrogenase" (2016). Honors Theses. 287.
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