Dr. David Barondeau will join the Department of Chemistry at Texas A&M University as an Assistant Professor in August 2006. Dr. Barondeau received his undergraduate degree from Southern Utah University (formerly Southern Utah State College). During his graduate work with Professor Paul Lindahl here at Texas A&M University, he applied biochemical and spectroscopic (EPR and Electronic Absorption) methods to elucidate mechanistic details for the metalloenzymes hydrogenase and acetyl-CoA synthase. As a Senior Research Associate at The Scripps Research Institute, Dr. Barondeau used protein crystallography, spectroscopy, and molecular biology to design and characterize protein-based metal ion biosensors, investigate the structure and mechanism of nickel superoxide dismutase, and understand the post-translational modification chemistry for chromophore biosynthesis in the green fluorescent protein.
The Barondeau laboratory at Texas A&M will couple protein crystallography with other biophysical, spectroscopic, and biochemical methods to elucidate chemical mechanisms for medically and environmentally important biological systems. In particular, his group will seek to understand detailed structure-function properties for proteins/enzymes involved in eukaryotic Fe-S cluster biogenesis, chlorophyll biosynthesis, and DNA repair in sporylating pathogens. Dr. Barondeau's research is at the interface of chemistry and biology and provides an excellent platform for interdisciplinary science and for training the next generation of scientists.
To learn more about the research being carried out in Dr. Barondeau's group, go to http://www.chem.tamu.edu/faculty/faculty_detail.php?ID=1422.