Research group leaders:

QIMR

 

University of Queensland Schools and Centres in which the research groups are located:

  • School of Chemistry & Molecular Biosciences (SCMB)
  • School of Biomedical Sciences (SBMS)
  • Centre for Magnetic Resonance (CMR)

 

sulfite dehydrogenase active site

Dr Ulrike Kappler - CMB Director

My research group is investigating bacterial metalloproteins involved in sulfur compound transformations. Both the proteins and the pathways involved in such reactions are still only partly understood. One main focus of our work are bacterial molybdenum containing enzymes that carry out a direct oxidation of sulfite to sulfate.

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Prof Paul Bernhardt

My group has a major research program in protein electrochemistry, particularly in the study of redox active enzymes from several families including the mononuclear Mo enzymes and the cytochromes P450. We are also involved in several projects that deal with the activity of iron chelators against certain diseases such as cancer and iron overload.

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Prof James De Voss

Cytochromes P450 are oxidative hemoproteins that catalyse a fascinating array of transformations which range from simple epoxidations all the way through to oxygen insertion into unactivated C-H bonds and C-C bond cleavage. P450s are essentially ubiquitous in nature and we have projects involved with several bacterial, fruit-fly and human P450s.

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Prof. Lawrie Gahan

My interests are in the role of transition metal complexes as drug delivery vehicles and also in the design of structural and functional models of enzyme active sites, in particular systems that catalyse phosphate ester hydrolysis reactions.

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Prof. Elizabeth Gillam

In humans cytochromes P450 are principally responsible for the clearance of a practically unlimited variety of chemicals from the body, but are also critical in many important physiological processes. Our research efforts take advantage of our expertise in the expression of recombinant human cytochrome P450 enzymes in bacteria. Our interests in this area combine a number of different approaches including characterising the active sites of these enzymes, so we can see how they can accommodate such substrate diversity yet retain in some cases quite specific regioselectivity, molecular breeding as a way of exploring sequence space and catalytic potential of P450 enzymes, the role of human P450s in the molecular toxicology of drugs and the role of human P450s in the metabolism of indole compounds in vivo.

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A/Prof Luke Guddat

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My research is focused on the three-dimensional structure determination of proteins using X-ray crystallography. I am currently involved in the study of several proteins that have biomedical applications including: purple acid phosphatase, 6-oxopurine phosphoribosyltransferase, acetohydroxyacid synthase and ketol-acid reductoisomerase.

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Prof. Graeme Hanson

My major research interests include continuous wave and pulsed EPR spectroscopy, its application to the characterisation of paramagnetic materials with special emphasis on the analysis of CW and pulsed EPR spectra and the metal binding sites in metalloproteins and transition metal ion complexes.

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Prof. Alastair.G. McEwan

The common research theme in my laboratory is the role of metals and oxidation-reduction processes in biocatalysis, regulation of gene expression, bacterial pathogenicity and in biotechnology. The microorganisms that we study include purple phototrophic bacteria, thermophilic archaea and bacterial pathogens.

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A/Prof Mark Riley

My current research interests centre on how the electronic states of a molecule influences its structure. An understanding of this is of fundamental importance to many of the dynamic molecular processes in chemistry and to molecular function in biology.

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A/Prof Gary Schenk

My research lies at the interface between biochemistry, inorganic and physical chemistry. Methodologies applied range from protein expression, purification and characterisation, steady- and pre-steady state enzyme kinetics and bioinformatics to molecular spectroscopy (cw and pulsed EPR, MCD and VTVH MCD, absorption and Raman) and density functional computations. More specifically, I am interested in the study of the reaction mechanisms of enzymes requiring transition metal ions for their catalytic function.

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Prof. Greg Anderson

My research lies at the interface between biochemistry, inorganic and physical chemistry. Methodologies applied range from protein expression, purification and characterisation, steady- and pre-steady state enzyme kinetics and bioinformatics to molecular spectroscopy (cw and pulsed EPR, MCD and VTVH MCD, absorption and Raman) and density functional computations. More specifically, I am interested in the study of the reaction mechanisms of enzymes requiring transition metal ions for their catalytic function.

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