Gunther, M.R. and Donahue, J.A. "Bicarbonate and active site zinc modulate the self-peroxidation of bovine copper-zinc superoxide dismutase", Free Radic. Res. 41:1005-1016, 2007.
Gunther, M.R., VanGilder, R., Fang, J., and Beattie, D.S. "Expression of a familial amyotrophic lateral sclerosis-associated mutant human superoxide dismutase in yeast leads to decreased mitochondrial electron transport". Arch. Biochem. Biophys. 431:207-214, 2004.
Gunther, M.R., Peters, J.A., and Sivaneri, M.K. "Histidinyl radical formation in the self-peroxidation reaction of bovine copper-zinc superoxide dismutase". J. Biol. Chem. 277, 9160-9166, 2002.
Gunther, M.R., Lardinois, O., Tschirret-Guth, R.A., and Ortiz de Montellano, P.R. "Tryptophan-14 is the preferred site of DBNBS spin trapping in the self-peroxidation reaction of sperm whale metmyoglobin". Chem. Res. Toxicol. 16:652-660, 2003.
Murray, E. Kisin, V. Castranova, C. Kommineni, M.R. Gunther, and A.A. Shvedova. "Phenol induced in vivo oxidative stress in skin: Evidence for enhanced free radical generation, thiol oxidation, and antioxidant depletion". Chem. Res. Toxicol. 20:1769-1777, 2007.
ALS - Amyotrophic Lateral Sclerosis
Dr. Gunther's research has been directed towards understanding how mutant forms of the protein superoxide dismutase cause the neurodegenerative disease amyotrophic lateral sclerosis (ALS). The primary interests of the lab have been identifying and characterizing free radicals formed on proteins with the hope of understanding how these unstable species might contribute to disease pathophysiology. In recent years we have been studying mitochondrial defects that arise from the expression of the ALS-causing mutant superoxide dismutase proteins in yeast. The main tools used in our laboratory are UV-visible spectroscopy and EPR spectroscopy, which is used to study free radicals.