Martin J. Stillman Professor Ph. D. University of East Anglia (Norwich, UK) PDF University of Alberta, Canada Office: Chemistry 064. Labs: Chemistry 051, 052, 055 Phone (Office): 519-661-3821 (ext 83821) Phone (Lab): 519-661-2111 ext 86358 stillman@uwo.ca Research Group Homepage

Mechanistic and electronic structure studies of bioinorganic systems. Studies using electrospray ionization mass spectrometry, magnetic circular dichroism, emission and emission lifetime techniques of metal-binding to proteins, porphyrins, heme proteins, the Isd proteins in Staphylococcus aureus, and metal-induced protein folding in metallothioneins.

Current Research Programs:

The general theme of using mass spectral, optical and NMR spectroscopic data to obtain mechanistic, functional, structural, or electronic state information for molecules of bioinorganic interest. Our research encompasses all aspects of the roles of metals in biology and of porphyrinoid electronic properties.

Metal binding properties of the protein metallothionein, using electrospray mass spectrometry, XAS, metal-NMR, EPR, circular dichroism and emission spectroscopy to determine speciation as the protein binds the metals As, Cd, Hg, Ag, Cu, and Au. Formation of Cu₁₂-MT, Ag₁₂-MT, Ag₁₈-MT, Hg₇-MT and Hg₁₈-MT have been reported. The mechanism for As(III) binding reported in 2006, represented the first kinetic analysis for a multi-metal-binding protein. Multi-domain proteins with biotechnological properties. Extensive use of molecular modelling provides an understanding of the spectroscopic data.

The redox and spectroscopic properties of phthalocyanines and porphyrins. Effects of symmetry-reduction through both peripheral substitution and porphyrin-ring folding. Electronic properties of porphyrinoids, to determine the electronic distribution and the effect on chemical properties. Calculations of the electronic structures of very large ring compounds to allow future prediction of chemical and physical properties..

Identifying methods to overcome antibiotic resistant S. aureus in humans. Studies of the iron-containing heme binding properties of a series of proteins located on the outer wall of the pathogenic bacterium, Staphylococcus aureus to discover means of overcoming the increasingly disturbing antibiotic resistance in S. aureus (MSRA) now in the general population. In 2008, we reported the first evidence that heme can be shuttled between the Isd proteins..

Selected Publications:

H. Kaluarachchi; D.E.K. Sutherland; A. Young; I.J. Pickering; M. J. Stillman; D.B. Zamble (2009) "The Ni(II)-binding properties of the metallochaperone SlyD", J. Am. Chem. Soc., 131, 18489-18500.

Ngu, T., Lee, J., Rushton, M.K., Stillman, M.J. (2009) "Arsenic-Metalation of Seaweed Fucus vesiculosus Metallothionein: The Importance of the Interdomain Linker in Metallothionein", Biochemistry, 48, 8806-8816.

Ngu, T.; Easton, A.; Stillman, M.J. (2008) "Kinetic analysis of arsenic-metalation of human metallothionein: Significance of the two-domain structure." J. Am. Chem. Soc., 130, 17016-17028.

Chan, J., Huang, Z., Watt, I., Kille, P., Stillman, M.J. (2008) "Metallobiological Necklaces: Mass Spectrometric and Molecular Modeling Study of Metallation in Concatenated Domains of Metallothionein", Chem. Eur. J., 14, 7579-7593.

Muryoi, N., Tiedemann, M.T., Pluym, M., Cheung, J., Heinrichs, D.E., Stillman, M.J. (2008) "Demonstration of the iron-regulated surface determinant (isd) heme transfer pathway in staphylococcus aureus", J. Biol. Chem., 283, 28125-28136.