Students with an interest in instrumentation development can pursue coupling EPR platform in situ electrochemistry, in situ gas exchange and in situ light (Solar, UV, LED, laser) excitation, allowing operando characterization of defects and their evolution.

This project aims to magnetically label proteins for new electron paramagnetic resonance (EPR) experiments to study a protein’s structure and dynamics at low concentrations and in-cell.

The project will involve training in the use of highly reactive, air-sensitive reagents, which require handling under strict anaerobic conditions. Furthermore, training in X-ray crystallography, multinuclear NMR spectroscopy and EPR spectroscopy will be given.

This project will magnetically label proteins for new electron paramagnetic resonance (EPR) experiments to study a protein’s structure and dynamics at low concentrations and in-cell, and then compute informative models from the measured EPR distances.

EPR and related double resonance techniques allow us to elucidate changes in the localization of electron density (metal or ligand centred) following reduction or oxidation, and thus predict likely routes of chemical reactions/catalysis.

Using Electron Paramagnetic Resonance spectroscopy we have been able to identify the sites of substrate water binding and important structural changes which facilitate substrate binding. We can now examine the formation of the last intermediate and the mechanism of O-O bond formation.