Electronic Structure of Metal-containing Systems

Most of the biochemical reactions that occur in the human body do not take place spontaneously - they require the presence of molecules called enzymes to occur at a significant rate.  Enzymes act as catalysts in reactions involved with processes such as the digestion of food, signal transduction and muscle contractions.  Malfunctioning enzymes can also lead to genetic diseases, and conditions such as mental impairment and cancer.

Andrew Dick and Associate Professor Mark Riley of the University of Queensland are concurrently performing spectroscopic and computational analysis in an effort to contribute to the understanding of enzymatic catalysis.  Experimentally they're performing a variety of spectroscopic techniques to determine the electronic and geometric structures of proteins of interest.

The researchers have been using QCIF facilities to run quantum chemistry computing programs to model the active sites of these proteins.

Participants

Andrew Dick, Associate Professor Mark Riley
School of Molecular and Microbial Sciences, UQ

Publications

M. Lanznaster et al.,  "A new heterobinuclear FeIIICuII complex with a Single Terminal FeIII-O(phenolate) bond. Relevance to purple acid phosphatases and nucleases", Journal of Biological Inorganic Chemistry, 2005, 10, 319-332.

E.G. Moore, P.V. Bernhardt, M.J. Riley and T.A. Smith, "Electronic energy-transfer rate constants for geometric isomers of a bichromophoric macrocyclic complex." Inorganic Chemistry, 2006, 45, 51-58.