Kathryn M McCulloch

Kathryn M McCulloch

Associate Professor, Chemistry and Biochemistry, College of Science

Biography

Appointments

Associate Professor, Chemistry & Biochemistry

Associate Chair, Chemistry & Biochemistry

Faculty Fellow for Program Review, Office of Assessment & Program Review

Education

Ph.D. Cornell University, Ithaca, NY

M.S. Cornell University, Ithaca, NY

B.S. (Chemistry) Ball State University, Muncie, IN

Postdoctoral Appointment

Vanderbilt University, Nashville, TN

Courses Taught

CHM 3270, Biochemistry I

CHM 3270L, Biochemistry I Laboratory

CHM 3280, Biochemistry II

CHM 3280L, Biochemistry II Laboratory

CHM 4520, Advanced Biomolecular Structure

CHM 4530, Informational Biomolecules & Recombinant DNA

CHM 5610, Advanced Topics in Biochemistry

CHM 5720, Current Advances in Inorganic Chemistry (co-taught with Dr. Stieber; Introduction to X-Ray Crystallography)

Research Interests

Overview

Organisms have not evolved in a vacuum – instead, they have interacted with their environment, competed for resources with other species, and collaborated with other organisms to thrive. These various forces have led to the evolution of complex pathways that produce signaling molecules, secondary metabolites, or otherwise provide the organism with an evolutionary advantage. To date, these pathways offer both the opportunity to develop new therapies, such as antibiotics, and offer potential targets for defeating pathogens or promoting human health. The McCulloch group aims to understand the chemistry of enzymes found within specific pathways. Currently, we are studying oxidoreductases (enzymes that catalyze either oxidations or reductions) encoded within the bile acid induced operon of some gut bacteria. We use a recombinant approach to overexpress each protein, and then use a combination of X-ray crystallography and in vitro biochemical assays to develop a molecular understanding of their structures and chemical reactivities.

Interactions between species

Bile Acid Metabolism

Our group is interested in understanding the transformation of primary bile acids - molecules synthesized in the liver and essential in the absorption of fat-soluble vitamins and nutrients, as well as important signaling molecules - into secondary bile acids by some species of gut bacteria. We use a recombinant approach to overexpress putative enzymes from this metabolic pathway and aim to determine the three-dimensional structures of these enzymes to answer important questions about how they work.