Department of Chemistry at The University of Montana

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Research Interests

My laboratory is devoted to the study of metalloproteins. My interests range from understanding metal ion homeostasis to studying the structure and function of metallo-proteins. The work is conducted in an atmosphere that emphasizes and exploits multidisciplinary approaches to research. Molecular biology techniques help to produce sufficient quantities of protein and allow structural variants to be made. Once protein is purified, the mechanistic and structural studies are carried out using a variety of spectroscopic techniques. These methods include UV-Vis, Atomic Absorption, Fluorescence, and Electron Paramagnetic Resonance (EPR) spectroscopies. When used to probe the active sites of metalloproteins or the metal-binding sites of chaperones, these techniques allow structure/function relationships to be discerned. The research covers a broad range of biochemistry techniques and interests.

One project studies the prion protein and related illnesses that include scrapie, mad cow disease, and Creutzfeld-Jakob disease. We seek to define the conformational changes that occur in the prion protein when it converts to the disease-causing state. We incorporate fluorescent amino acid analogs into the recombinant protein to monitor the conformational changes. Prions bind copper with high affinity and a role for copper in both the normal function of prions and in the coversion process has been proposed. We wish to elucidate any changes in the copper binding sites that occur as a result of conversion to the diseased state.

In a second project, my laboratory examines how amino acid radicals mediate long range electron transfer reactions in proteins. Azurin, a small blue copper protein, and cytochrome c', a heme-containing protein, serve as the model proteins for this study. This project involves electrochemistry and also uses amino acid analog incorporation, as a way of modulating the reduction potentials of the amino acid radicals.

Representative Publications

Lennon, C.W., Cox, H.D., Hennelly, S.P., Chelmo, S.J. and McGuirl, M.A. (2007). Probing structural differences in prion protein isoforms by tyrosine nitration. Biochemistry, 46, 4850-48.

Machczynski, M.C., Kuhl, K.P. and McCuirl, M.A. (2007). Modulations of the electrochemical behavior of tyrosyl radicals by the electrode surface. Anal Biochem. 362, 89-94.

Gray, E.E., Small, S.N. and McGuirl, M.A. (2006). Expression and characterization of recombinant tyramine beta- monooxygenase from drosophila: a monomeric copper-containing hydroxylase. Prot Exp Purif. 47, 162-170.

Taubner, L.M., McGuirl, M.A., Dooley, D.M., Copie, V. (2006). Structural studies of Apo-NosL, an accessory protein of the nitrous oxide reductase system: insights from structural homology with MerB, a mercury resistance protein. Biochemistry. 45, 12240-12252.

McGuirl, M.A. & Dooley, D.M. (2005). Copper proteins with type 2 sites. In R.B. King (Ed.) Encyclopedia of Inorganic Chemistry, New York: Wiley.

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Department of Chemistry  The University of Montana Missoula, MT 59812  (406) 243-4022  Fax: (406) 243-4227

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