David Harrison Professor (secondary appointment in Biochemistry) Dr. Harrison is a 1983 graduate of Emory University in Atlanta, GA where he received both his B.S. degree and M.S. degree in Chemistry. He then attended graduate school at Yale University in New Haven, CT, receiving his M. Phil degree in 1985 in the Department of Molecular Biophysics and Biochemistry. After two years working in the Protein Engineering Department at Eastman Kodak in Rochester, NY, he returned to the Yale University Department of Molecular Biophysics and Biochemistry to complete his Doctorate degree in 1992. From 1992 to 1995 he was a Juvenile Diabetes Foundation International postdoctoral fellow at the Rosenstiel Basic Medical Sciences Research Center at Brandeis University in Waltham, MA, where he initiated X-ray structural studies of Aldose Reductase. Dr. Harrison joined the faculty of the Medical College of Wisconsin in 1995 where he rose to the position of associate professor. Dr. Harrison joined the faculty of Biochemistry and Molecular Biology at The Chicago Medical School in 2003. Phone: (847) 578-8609 Fax: (847) 578-3240 Email: David.Harrison@rosalindfranklin.edu

My research interests are primarily focused on issues of molecular recognition in the cause and treatment of debilitating microbial diseases. I have recently been appointed to the position of associate professor in the Department of Biochemistry and Molecular Biology at the Rosalind Franklin University. Previously, I was a Juvenile Diabetes Foundation Post-Doctoral Fellow in the Rosenstiel Center at Brandeis University. That experience allowed me to enter into a very productive collaboration on aldose reductase with Dr. Ken Gabbay and Dr. Kurt Bohren of the Baylor College of Medicine in Houston, TX. Currently, My laboratory is working on understanding the enzymatic and allosteric mechanisms of Methylglyoxal Synthase from E. coli and B. subtlis. We have determined the structure of the E. coli enzyme to a resolution of 1.8 Angstroms, and we are refining the structure of the B. subtilis enzyme at a resolution of 1.3 Angstroms, and we hope to get neutron diffraction data on this enzyme. Additionally, my laboratory is working on understanding the mechanism and inhibition of hydroxymethylglutaryl-CoA (HMG-CoA) synthase from S. aureus (a major source of hospital borne infection).

Last updated by Correll November 2, 2010