Michael R. Gunther
Department of Biochemistry and Molecular Pharmacology
West Virginia University School of Medicine
Morgantown
WV 26506
USA
Name/email consistency: high
- Bicarbonate and active site zinc modulate the self-peroxidation of bovine copper-zinc superoxide dismutase. Gunther, M.R., Donahue, J.A. Free Radic. Res. (2007)
- Probing the free radicals formed in the metmyoglobin-hydrogen peroxide reaction. Gunther, M.R. Free Radic. Biol. Med. (2004)
- Expression of a familial amyotrophic lateral sclerosis-associated mutant human superoxide dismutase in yeast leads to decreased mitochondrial electron transport. Gunther, M.R., Vangilder, R., Fang, J., Beattie, D.S. Arch. Biochem. Biophys. (2004)
- Tryptophan-14 is the preferred site of DBNBS spin trapping in the self-peroxidation reaction of sperm whale metmyoglobin with a single equivalent of hydrogen peroxide. Gunther, M.R., Tschirret-Guth, R.A., Lardinois, O.M., Ortiz de Montellano, P.R. Chem. Res. Toxicol. (2003)
- Histidinyl radical formation in the self-peroxidation reaction of bovine copper-zinc superoxide dismutase. Gunther, M.R., Peters, J.A., Sivaneri, M.K. J. Biol. Chem. (2002)
- A long-lived tyrosyl radical from the reaction between horse metmyoglobin and hydrogen peroxide. Gunther, M.R., Sturgeon, B.E., Mason, R.P. Free Radic. Biol. Med. (2000)