Activating Biological Functions in Proteins using Gas Sensing Molecules

Faculty Sponsor

Robert Clark


Arts and Sciences


Chemistry Department

Presentation Type

Poster Presentation

Symposium Date

Summer 7-31-2014


Heme proteins are a class of biological molecules that serve important roles throughout all forms of life. The protein studied in this research, CooA, is found in several bacteria such as Rhodospirillum rubrum (Rr) and Carboxydothermus hydrogenoformans (Ch). In nature, all forms of CooA sense a specific gas molecule, carbon monoxide, that allows the heme protein to bind DNA which activates the transcription process. Interestingly however, in the lab nitric oxide has also been found to activate DNA binding in Ch CooA, but it does not activate Rr CooA. It is hypothesized that a specific intermolecular interaction between amino acids within the heme environment is responsible for the different behavior of Ch CooA and Rr CooA. To test this hypothesis, the key amino acids that are proposed to be responsible for this interaction were mutated in both CooA proteins. Next, these variant CooA proteins will be reacted with carbon monoxide and nitric oxide, and the subsequent effects on DNA binding will be measured.

Biographical Information about Author(s)

Rachael DeVries is a freshman Chemistry-Biology double major from St. Charles, Illinois who enjoys swimming and rock music. She is looking forward to attending medical school after she graduates. This summer is Rachael's first year on the project. Jessica Lyza is a senior Biochemistry major from Schererville, Indiana who enjoys running and playing ultimate frisbee. She will be applying to medicinal biochemistry graduate school programs in the fall in the hopes to attend graduate school next year. Jessica has been working on this project since her second semester sophomore year.

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