Department of Chemistry and Biochemistry


Donald R. Ronningronning
Office: WO 2256B
Phone: (419) 530-1585
Lab: (419) 530-1588
Fax: (419) 530-4033

Professional Background:
B.S., Biochemistry, 1995, University of Minnesota
Ph.D., 2001, Texas A&M University
Research Fellow, 2001-2005, National Institutes of Health

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Research Synopsis:

Trehalose Metabolism - Trehalose is profoundly important for the survival and virulence of M. tuberculosis (figure below). We are studying the essential otsAB biosynthetic pathway responsible for the de novo synthesis of trehalose and may play a role in the biosynthesis of trehalose monomycolate, which is an essential donor molecule required for the building of the Mycobacterial outer membrane (mycomembrane). Since the antigen 85 enzymes use trehalose monomycolate as a substrate to transfer mycolic acids to the mycomembrane and are essential for the viability of M. tuberculosis, we are studying their enzymatic activity, substrate specificity, and post-translational modification in collaboration with Steve Sucheck (University of Toledo), Mary Jackson (Colorado State University) and Choong-min Kang (University of California-Stanislaus). Finally, we are studying the GlgE maltosyltransferase, which functions in the trehalose recycling branch of this pathway and is a genetically validated TB drug target. 

trehalose pathway

Mycobacterial Redox Homeostatis -  As a consequence of our recent work identifying the mechanism of action of Antigen 85 Complex inhibition by ebselen, we have recently started studying systems used by M. tuberculosis to modify drug molecules and promote their efflux from the mycobacterial cytoplasm. One important compound produced at high level by mycobacteria is Mycothiol. Disrupting the biosynthesis and utilization of Mycothiol in mycobacteria will disrupt redox homeostasis and prevent its availability to detoxify anti-tubercular drugs. This project is through a collaboration with Peter Andreana's lab (University of Toledo).



Last Updated: 12/29/16