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
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:
Tiedemann, M.; Heinrichs, D.E.; Stillman, M.J. (2012) "The multi-protein heme shuttle pathway in Staphylococcus aureus: Isd cog-wheel kinetics", J. Am. Chem. Soc. 134, 16578-16585. DOI: 10.1021/ja305115y.
Tiedemann, M.T.; Pinter, T.B.J.; Stillman, M.J. (2012) "Insight into blocking heme transfer by exploiting molecular interactions in the core Isd heme transporters IsdA-NEAT, IsdC-NEAT and IsdE of Staphylococcus aureus", Metallomics, 4, 751-760. DOI: 10.1039/C2MT20067H (featured on cover). (TOP 10 downloads in July, 2012)
Sutherland, D.E.K.; Summers, K.L; Stillman, M.J. (2012) "Noncooperative metalation of metallothionein 1a and its isolated domains", Biochemistry, 51: 6690-6700. DOI: /10.1021/bi3004523,
Sutherland, D.E.K.; Willans, M.J.; Stillman, M.J. (2012) "Single domain metallothioneins: Supermetalation of human MT 1a", J. Am. Chem. Soc., 134, 3290-3299.
