Michael J. Reddish

Dr. Reddish earned a B.S. in chemistry from Furman University in 2009 and a Ph.D. in chemistry in 2015 from Emory University. As an undergraduate he performed biophysical chemistry research with Dr. Jeff Petty on the structure of trinucleotide repeat sequences associated with certain genetic disorders. His graduate research work with Dr. Brian Dyer focused on fundamental questions about how enzymes function. Specifically, he was interested in the role that conformational changes in enzymes’ protein structures play in catalysis. To accomplish this work, he developed instrumentation to observe these fast processes utilizing various laser-based spectroscopic techniques. After graduate school, Dr. Reddish moved to Vanderbilt University to study cytochrome P450 enzymes with Dr. F. Peter Guengerich.  Dr. Reddish’s work focused on how human cytochrome P450 enzymes metabolize natural steroids.  Dr. Reddish joined the department of chemistry at Appalachian State University in 2019 and teaches classes in Biochemistry, Analytical, and Introductory Chemistry.

Current research projects in the Reddish lab utilize biochemical, analytical, and spectroscopic techniques to investigate steroid enzymology.  The Reddish lab is particularly interested in trying to understand how regions of an enzyme’s structure far away from the active site of the enzyme, so called allosteric sites, contribute to catalysis.  The current approach for these investigations is to study how naturally-occurring variants of human P450s are able to function.  Enzymes are made up of specific sequences of hundreds of amino acids that determine both their three-dimensional structure and function.  Often, when just one of these amino acids is changed, enzymes can have altered functionality or none of their original functionality at all.  We are investigating how single amino acid substitutions of the enzymes cytochrome P450 11B2 (aldosterone synthase) and cytochrome P450 27A1 (sterol 27-hydroxylase) that exist normally in some people alter the abilities of these enzymes to function.  We hope that with a better understanding of how allosteric sites contribute to enzyme catalysis, medical treatments that target these enzymes can be more optimally produced.  Undergraduate research students in the lab utilize techniques including recombinant protein expression & purification, enzymes kinetics, optical spectroscopy, and HPLC-UV-MS.  Interested students are encouraged to contact Dr. Reddish to inquire about working in the lab.

Title: Assistant Professor
Department: Department of Chemistry and Fermentation Sciences

Email address: Email me

Phone: (828) 262-2159

Office address
401 Garwood Hall
Mailing address
525 Rivers Street, Boone, NC 28608