The Influence of pH Variation on CooA Activity

Faculty Sponsor

Dr. Robert Clark


Arts and Sciences



ORCID Identifier(s)

0000-0003-3030-725X (Rachael DeVries), 0000-0001-6991-014X (Brian Weaver)

Presentation Type

Poster Presentation

Symposium Date

Summer 7-28-2015


A bacterial heme protein, CooA, changes shape to bind DNA and activate transcription. Previous research indicated gas molecule (e.g. carbon monoxide) binding to CooA is essential to initiate protein shape change, but recent studies suggested the protein may be able to bind DNA without gas in acidic conditions. To investigate this, CooA was subjected to an acid range of 4-10 pH units and DNA binding was measured via a fluorescence anisotropy assay. From these studies, pH dependent DNA binding was observed, and optimal binding was achieved in the pH 4-6 range. Addition of gas did not improve DNA binding at these pH values. Ongoing studies are investigating the molecular basis of this effect.

Biographical Information about Author(s)

Rachael DeVries is a junior biology and chemistry major, and has been doing research on CooA for a little over a year. As an aspiring medical student, she found the biochemical basis of the project and the subject (heme proteins) to be intriguing. She hopes to continue working on this project into the school year, and would like to achieve publication worthy results.

Brian Weaver is a junior biochemistry major. He started on this particular project at the end of June 2015. Brian is an ambitious student, whose thirst for knowledge is tough to match. He finds CooA research especially appealing due to the fact that it combines two seemingly unrelated fields, inorganic and biological chemistry. His future career plans include attending graduate school to study biochemistry. Like Rachael, he hopes to continue on the project into the school year, publish in a reputable journal as well as speak at a biochemistry conference during the upcoming spring semester.

This document is currently not available here.