Shelagh Ferguson-Miller
University Distinguished Professor
- Chairperson, MSU Biochemistry, 2003 - 2008
- MSU Distinguished Professor, 1997
- Research Associate, Northwestern University, 1972-77
- Fellow of Canadian National Research Council, Oxford, 1971-72
- Ph.D., University of Wisconsin, Madison, 1971
- M.A., University of Toronto, 1966
fergus20@msu.edu
210 Biochemistry Building
Michigan State University
East Lansing, MI 48824-1319
Office: 517-355-0199
Lab: 517-353-3512
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Shelagh Ferguson-Miller
Research Interests
Electron transfer
coupled to proton translocation is the basic mechanism of energy
generation in most living organisms, but the molecular mechanism is not
understood. A key enzyme in all eukaryotic and most prokaryotic electron
transfer systems is cytochrome c oxidase, 
which accepts electrons
derived from food and donates them to oxygen, generating a pH and
electrical gradient to drive ATP synthesis.
We are studying mammalian,
plant and bacterial cytochrome c oxidases which differ in peptide
composition but carry out the same reactions using the same metal centers
to catalyze the process. Each of these enzymes offers different advantages
for investigating the molecular mechanism of energy transduction by a
variety of approaches, including kinetic analysis, chemical modification,
physical/spectral techniques, genetic engineering and crystallography. To
understand the molecular basis of electron transfer and coupled proton
translocation, mutants have been prepared in highly conserved residues
predicted to be metal ligands or proton ligands. MORE
Recent Publications
Qin L, Sharpe MA, Garavito RM, Ferguson-Miller S. Conserved lipid-binding sites in membrane proteins: a focus on cytochrome c oxidase. Curr Opin Struct Biol. 2007 Aug;17(4):444-50. Review.
Qin L, Mills DA, Hiser C, Murphree A, Garavito RM, Ferguson-Miller S, Hosler J. Crystallographic location and mutational analysis of Zn and Cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome c oxidase. Biochemistry. 2007 May 29;46(21):6239-48.
Xu J, Sharpe MA, Qin L, Ferguson-Miller S, Voth GA. (2007) Storage of an excess proton in the hydrogen-bonded network of the d-pathway of cytochrome C oxidase: identification of a protonated water cluster. J Am Chem Soc. 129(10):2910-3.
Qin L, Hiser C, Mulichak A, Garavito RM, Ferguson-Miller S. (2006) Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase. Proc Natl Acad Sci U S A. 103(44):16117-22.
Hosler JP, Ferguson-Miller S, Mills DA. (2006) Energy transduction: proton transfer through the respiratory complexes. Annu Rev Biochem. 75:165-87.
Seibold SA, Mills DA, Ferguson-Miller S, Cukier RI. (2005) Water chain formation and possible proton pumping routes in Rhodobacter sphaeroides cytochrome c oxidase: a molecular dynamics comparison of the wild type and R481K mutant. Biochemistry. 44(31):10475-85.
Branden G, Branden M, Schmidt B, Mills DA, Ferguson-Miller S, Brzezinski P. (2005) The protonation state of a heme propionate controls electron transfer in cytochrome c oxidase. Biochemistry. 44(31):10466-74.
Mills DA, Geren L, Hiser C, Schmidt B, Durham B, Millett F, Ferguson-Miller S. (2005) An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase. Biochemistry. 44(31):10457-65.MORE