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Electrochemical insights into redox-active metalloproteins, bacterial metabolism and catalysis
I am interested in how oxidation state changes at transition metal centres in proteins activate chemical reactions which are essential for life. Understanding such processes is important across a wide range of fields: a fundamental understanding of how bacteria derive the energy for life is essential if we are to develop new antibiotics to halt the rise in drug-resistant pathogens; learning how H2 and other small molecule activation occurs efficiently and rapidly at non-precious metal centres teaches us how to design better industrial catalysts; and finding out how novel proteins function in humans reveals how we work as big reaction vessels of living chemistry.
In the laboratory the main technique used to interrogate these redox reactions is film electrochemistry. This method permits precise control of the reduction-potential of the protein so that measurement of current provides a quantitative measure of the rate of redox reactions. Thermodynamic and kinetic reaction parameters are determined quantitatively, and enzymatic reaction mechanisms can be probed through analysis of substrate catalysis and inhibitor sensitivity. To complement the functional insight that electrochemistry provides, structural information is determined with molecular biology, protein crystallography, electron paramagnetic resonance and infra-red spectroscopy.