Faculty Investigator: Robert Hondal, PhD
Associate Professor of Biochemistry and Chemistry
Dr. Hondal received a B.S. in chemistry from the University of Pittsburgh (1991). His graduate work was in mechanisitic enzymology in the Department of Chemistry at The Ohio State University (Ph.D. chemistry, 1997). While he was a graduate student he became interested in both protein engineering and the 21st amino acid in the genetic code, selenocysteine. He did one year of post-doctoral studies at Vanderbilty University, where he studied a selenium transport protein. Following his stint at Vanderbilt, Dr. Hondal moved to the University of Wisconsin-Madison, where he combined his love of protein engineering and selenocysteine and developed a method to make selenium-containing proteins by semisynthesis. He applied this technique to thioredoxin reductase, a key enzyme in mediating redox homeostasis in the cell. Since then, the Hondal lab has been studying the mechanism of this enzyme as well as their key question: Why did Nature choose selenium?Members:
~Drew Barber – 3rd year graduate student (Ph.D. candidate)
~Christopher Dustin – laboratory technician (and incoming CMB student)
~John O’Keefe – senior biochemistry major (thesis)
~Zachary Ehret – senior biochemistry major
~Connor Payne – sophomore chemistry major (thesis)
~Erik Ruggles – Ph.D. Research Associate
Accepting rotation students: Yes
Major Research Projects: Major projects in the Hondal lab include: (i) Which chemical property of selenium is needed to make thioredoxin reductase and other selenoenzymes work? (mechanistic enzymology), (ii) The synthesis of a new selenocysteine analog that we hope to use as a drug to treat COPD and other diseases involving redox imbalance, (iii) Which chemical property of selenium explains its use in biology? Their hypothesis is that it imbues enzymes with the ability to resist irreversible inactivation by oxidation. They are currently exploring one-electron redox reactions as a special property that selenium confers to an enzyme.
Exciting News in the Hondal Lab:
- Work by Hondal Lab Alumnus Gregg Snider published in Biochemistry (Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: Comparison of selenium and sulfur enzymes, Biochemistry 2013, 52, pp 5472–5481) was spotlighted in Chemical Research in Toxicology.
- A second paper by Hondal Lab Alumnus Adam Lothrop (Why is mammalian thioredoxin reductase-1 so dependent upon the use of selenium? Biochemistry 2014, 53, 554-564.) was highlighted on the Biochemistry web site by the Editor.