1. Biomedical EPR Facility at the University of Essex Dima Svistunenko Cover your research questions Mechanism of action of enzymes and proteins. Globins: We have extensive experience in studying different globins (extremely useful for elucidation the structure / function relationships) Globins bind oxygen and they can be damaged by oxygen – it is important to understand when and how this happens Artificial blood (haemoglobin based blood substitutes) Oxidative stress in general One unique globin is also an enzyme – dehaloperoxidase (DHP)

2. Cover your research questions One unique globin is also an enzyme – dehaloperoxidase (DHP) DHP – how can it have two functions normally performed by enzymes of opposing properties? KatG – another bi-functional enzyme; directly related to tuberculosis resistance to most effective drug Haptoglobin – how does it make Hb non-toxic? Cyt c’ - how can it bind NO and CO, but not O 2 ? How can theoretical models produce a method of pin-pointing the radical site in a protein from experimental EPR spectrum of the radical and the 3D structure of the protein?

3. Methods/techniques EPR spectroscopy Optical spectroscopy Kinetic studies by both optical and EPR spectroscopies RFQ method for EPR sampling Mathematical models of kinetic data (10+ components) DFT calculation of models and PDB structures

4. Envisaged collaborations (on-going, actually) Internal: Jonathan Worrall (DHP, KatG, cyt c, copper proteins in Streptomyces) Mike Hough (DHP, cyt c’ from different sources) Brandon Reeder (cytoglobin, neuroglobin, plant haemoglobins) Chris Cooper (human Hb mutants) External: Reza Ghiladi, North Carolina State University (Dehaloperoxidase, DHP) Nick Le Brun, UEA (Bacterioferritin, BFR) Sylvia Dewilde, University of Antwerp (fish myoglobins) John Bartington, Technologica (new freeze-quench machine)