Bruce C. Hill, Ph.D

Bruce C. Hill
  • Associate Professor
  • Botterell Hall, Room 628/633
  • Kingston
  • K7L3N6
  • Telephone: 613-533-6375
  • E-Mail:

Faculty Bio

I am interested in describing the molecular mechanism of O2 reduction, and in the details of energy transduction. Since these enzymes employ the transition metals iron and copper during catalysis a variety of spectroscopic approaches are used to characterize the status of these functional groups and their surrounding protein environments. We use transient-state optical spectroscopy to define elementary steps in O2 reduction, and this approach is being extended to study the transmembrane reactions involved in energy transduction. We also use electron paramagnetic resonance to characterize further the transition metals and to look at the role of protein-based free radicals as intermediates in these reactions. We use purified cytochrome c oxidases from heart muscle mitochondria and from the respiratory chain of the aerobic bacterium Bacillus subtilis. We are also studying a putative copper chaperone protein, known as SCO, that is involved in the assembly of cytochrome c oxidase. This work is focused on the B. subilis homolog of SCO (i.e., BsSCO). We employ site-directed mutagenesis on recombinant BsSCO to look at structure and function relationships in terms of metal binding and redox properties.

Last Modified: 2012-10-19