UM Directory

Bruce Bowler joined the University of Montana in 2006 as Professor of Chemistry and a member of the Center for Biomolecular Structure and Dynamics.  He received his Ph. D. degree in 1986 with Stephen J. Lippard at the Massachusetts Institute of Technology.  From 1986 to 1989, he was a Medical Research Council of Canada postdoctoral fellow in the laboratories of Harry Gray and Jack Richards at the California Institute of Technology.  From 1989 to 2006 he was a professor of chemistry at the University of Denver.  Dr. Bowler is a physical biochemist with interests in protein folding, the conformational restraints that specify the protein folding code and protein dynamics as applied to the conformational changes that mediate the function of cytochrome c in apoptosis.  Dr. Bowler is currently the Interim Dean of the College of Science and the Director of the Center for Biomolecular Structure and Dynamics.

Education

B.S. in Chemistry, Brown University, Providence, RI, 1981

M.S. in Chemistry, Columbia University, New York, NY, 1982

Ph.D. in Chemistry, MIT, Cambridge, MA, 1986

Postdoctoral Fellow, Chemistry, Caltech, Pasadena, CA, 1986-1989

Courses Taught

BCH 480 Advanced Biochemistry I

Research Interests

Research in the Bowler lab focuses on two areas: protein folding and the relationship between protein conformational dynamics and function. 

Our work on protein folding emphasizes the conformational biases inherent in protein denatured states that bias the free energy landscape of a protein toward its native conformer. The ultimate goal of this research is to understand the physical basis of the protein folding code.    

Our work on the relationship between protein conformational dynamics and function focuses on the structural factors that control access to conformers of mitochondrial cytochrome c  which permit peroxidase activity. Under conditions of oxidative stress cytochrome c oxygenation of the inner mitochondrial membrane lipid, cardiolipin, provides the earliest signal in the intrinsic pathway of apoptosis. A key goal of this work is to understand how cytochrome c has evolved to become a regulatory on/off switch for apoptosis.

Selected Publications

Bandi, S., and Bowler, B. E. (2026) Mutation of Pro76 affects the dynamics of Ω-loop D of yeast Iso-1-cytochrome c: Application of gated electron transfer, J. Inorg. Biochem. 280, 113296, https://doi.org/10.1016/j.jinorgbio.2026.113296.

Bosco, J., Gagliano, E., Boshae, K., Statz, J., Wheeler, T., Cuello, D., Sliter, A., Newby, C., Lin, B., Demeler, A., Pierpont, C. L., Yates-Hansen, C., Sydor, M., Ferrini, M. E., Kuch, K. C., Cooper, B., Piggott, B. J., Certel, S. J., Hansen, K. B., Sprang, S., Bruce Bowler, B., McClelland L., Berkmen. M., and Voronina, E. (2025) A galactose-based auto-expression system improves T7-inducible protein production in Escherichia coli. Sci. Rep. 15, 8936, https://doi.org/10.1038/s41598-025-91954-5.

Frederick, A. K.,* and Bowler, B. E. (2024) Binding of yeast and human cytochrome c to cardiolipin nanodiscs at physiological ionic strength, J. Inorg. Biochem. 260, 112699, https://doi.org/10.1016/j.jinorgbio.2024.112699.

Martin, W. J., McClelland, L. J., Nold, S. M., Boshae, K. L., and Bowler, B. E. (2024) Effect of proline content and histidine ligation on the dynamics of Ω-loop D and the peroxidase activity of iso-1-cytochrome c, J. Inorg. Biochem. 252, 112474, https://doi.org/10.1016/j.jinorgbio.2023.112474.

Rothfuss, M. T., Becht, D. C., Zeng, B., McClelland, L. J., Yates-Hansen, C., and Bowler, B. E. (2023) High-accuracy prediction of stabilizing surface mutations to the three-helix bundle, UBA(1), with EmCAST, J. Am. Chem. Soc. 145, 22979-22992, https://doi.org/10.1021/jacs.3c04966.

Van Gundy, T., Patel, D., Bowler, B. E., Rothfuss, M. T., Hall, A. J., Davies, C., Hall, L. S., Drecktrah, D., Marconi, R. T., Samuels, D. S., and Lybecker, M. C. (2023) c-di-GMP regulates activity of the PlzA RNA chaperone from the Lyme disease spirochete, Mol. Microbiol. 119, 711-727, https://doi.org/10.1111/mmi.15066

Lei, H., Kelly, A. D., and Bowler, B. E. (2022) Alkaline state of the domain-swapped dimer of human cytochrome c: a conformational switch for apoptotic peroxidase activity, J. Am. Chem. Soc. 144, 21184-21195, https://doi.org/10.1021/jacs.2c08325.

Frederick, A. K., Thompson, S. L., Vakharia, Z. M., Cherney, M. M., Lei, H., Evenson, G., and Bowler, B. E. (2022) Effect on intrinsic peroxidase activity of substituting coevolved residues from Ω-loop C of human cytochrome c into yeast iso-1-cytochrome c, J. Inorg. Biochem. 232, 111819, https://doi.org/10.1016/j.jinorgbio.2022.111819.

Becht, D. C., Leavens, M. J., Zeng, B., Rothfuss, M. T., Briknarová, K., and Bowler, B. E. (2022) Residual structure in the denatured state of the fast-folding UBA(1) domain from the human DNA excision repair protein HHR23A, Biochemistry 61, 767–784, https://doi.org/10.1021/acs.biochem.2c00011.

Leavens, M. J., Spang, L. E., Cherney, M. M., and Bowler, B. E. (2021) Denatured state conformational biases in three-helix bundles containing divergent sequences localize near turns and helix capping residues, Biochemistry 60, 3071−3085, https://doi.org/10.1021/acs.biochem.1c00400.

Steele, H. B. B., Elmer-Dixon, M. M., Rogan, J. T., Ross, J. B. A., and Bowler, B. E. (2020) The human cytochrome c domain-swapped dimer facilitates tight regulation of intrinsic apoptosis, Biochemistry 59, 2055-2068, https://doi.org/10.1021/acs.biochem.0c00326.

Elmer-Dixon, M. M., Xie, Z., Alverson, J. B., Priestley, N. D., and Bowler, B. E. (2020) Curvature dependent binding of cytochrome c to cardiolipin, J. Am. Chem. Soc. 142, 19532-19539, https://dx.doi.org/10.1021/jacs.0c07301.

Publications

Complete list of publications.

Research Summary

Protein folding and conformationally-gated electron transfer reactions in proteins

CBSD Facilities

Facility

Specialized Research Interests

Protein folding, conformationally-gated electron transfer and structural biology of cytochromes.

Chair Director Departments

Center for Biomolecular Structure and Dynamics