Title

Synthesis of Functional Catalysts for the Conversion of Toxic Carbon Monoxide Based on a Bacterial Protein

Abstract

An estimated 100 million tons of atmospheric carbon monoxide is removed by the soil bacteria Oligotropha carboxidovorans, containing the CO dehydrogenase enzyme. The enzyme catalyzes the conversion of CO and water to carbon dioxide and hydrogen gas, which is analogous to the industrial water-gas shift reaction used for hydrogen gas production. The industrial process requires elevated temperatures and pressures, whereas the bacteria can carry out the reaction under ambient conditions. We aim to understand the structure and function of the CODH enzyme and its ability to carry out this reaction. The reaction center of the enzyme is composed of molybdenum and copper metals surrounded by additional protein components. We are using computational and experimental techniques to design and synthesize metal complexes similar to this reaction center.

Faculty Sponsor

Dalia Rokhsana

Tracks

poster

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Location

Cordiner Hall

Presentation Type

Poster

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Synthesis of Functional Catalysts for the Conversion of Toxic Carbon Monoxide Based on a Bacterial Protein

Cordiner Hall

An estimated 100 million tons of atmospheric carbon monoxide is removed by the soil bacteria Oligotropha carboxidovorans, containing the CO dehydrogenase enzyme. The enzyme catalyzes the conversion of CO and water to carbon dioxide and hydrogen gas, which is analogous to the industrial water-gas shift reaction used for hydrogen gas production. The industrial process requires elevated temperatures and pressures, whereas the bacteria can carry out the reaction under ambient conditions. We aim to understand the structure and function of the CODH enzyme and its ability to carry out this reaction. The reaction center of the enzyme is composed of molybdenum and copper metals surrounded by additional protein components. We are using computational and experimental techniques to design and synthesize metal complexes similar to this reaction center.

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