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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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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My research focuses primarily on the chemistry of noble metals, including the biological chemistry of platinum complexes related to platinum-based antitumour agents, and the interactions of noble metal compounds with amino acids and peptides, with special emphasis on those biological molecules containing sulfur donors, which have high affinity for platinum.

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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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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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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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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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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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My research investigates the role of metals in amyloidogenic diseases such as Mad Cow disease and Alzheimers. Specifically, we focus on the role of copper in these diseases and the role of copper in the brain. Further research avenues explore the use of copper in enhancing immunosuppressant efficacy and reducing side-effects.

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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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My research lies at the interface between biochemistry, inorganic and physical chemistry. Specifically I am interested in the study of the reaction mechanisms of enzymes requiring transition metal ions for their catalytic function. My current research includes studies on binuclear metallohydrolases and cytochromes P450. Some of the physical methods we employ include molecular spectroscopy, computational chemistry, stopped flow spectrophotometry and bioinformatics in addition to recombinant protein expression and purification techniques.

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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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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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My research group is investigating the molecular biology, biochemistry, and ecology of bacterial manganese oxidation by Pedomicrobium, Leptothrix, and Pseudomonas.  We have recently discovered that a novel form of membrane-bound multicopper oxidase is essential for manganese oxidation and laccase-like activity in Pedomicrobium and we are investigating the heterologous expression of this protein for further biochemical characterisation.  We are also investigating the relationship between biofilm formation and the regulation of manganese oxidation in Pedomicrobium.  This work will be aided by the forthcoming genome sequence of Pedomicrobium manganicum.  The knowledge derived from this research is being applied to understanding the cause and control of manganese oxidation and deposition in water distribution systems and to the development of an up-flow bioreactor for use in the treatment of manganese in drinking water and to the development of a biotechnology process for the removal of heavy metals and radionuclides from industrial effluents.

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