Professor Johnson received B.A. (1974) and M.A. (1977) degrees from Cambridge University, England, and M.S. (1975) and Ph.D. (1978) degrees from the University of East Anglia, England. He was a U. K. Science Research Council Postdoctoral Fellow at the University of East Anglia and came to the U. S. in 1980 as a postdoctoral research associate at Princeton University. Before joining the faculty in 1987, he was an Assistant and Associate Professor at Louisiana State University and an Alfred P. Sloan Research Fellow . He is currently co-director of the Center for Metalloenzyme Studies at the University of Georgia. His research interests encompass bioinorganic, biophysical, and bioanalytical chemistry.
Our research concerns the role and properties of transition metal centers in metalloenzymes and metalloproteins. Metal ions carry out a wide variety of roles in biology, e.g. electron transport, catalytic, structural, gene regulation, organic radical generation/stabilization, and elucidating structure/function relationships offers a fascinating challenge to inorganic and physical chemists. To accomplish this goal, we use a range of spectroscopic techniques (electron paramagnetic resonance, resonance Raman, UV-visible absorption, natural and magnetically induced circular dichroism), in order to elucidate the electronic, magnetic, and structural properties of biological metal centers. The current foci of our research program are iron-sulfur, heme, nickel, cobalt, molybdenum, and tungsten centers in a range of proteins and enzymes.
M.T. Werth, S-F. Tang, G. Formicka, M. Zeppezauer, and M.K. Johnson, "Magnetic Circular Dichroism and Electron Paramagnetic Resonance Studies of Cobalt-Substituted Horse Liver Alcohol Dehydrogenase", Inorg. Chem. 1995, 34, 218.
H.A. Dailey, M.G. Finnegan and M.K. Johnson, "Human Ferrochelatase is an Iron-Sulfur Protein", Biochemistry 1994, 33, 403.