Redox reactions underpin innumerable chemical reactions - and much of the chemistry of life! I am fascinated by how oxidation-state changes govern respiration and photosynthesis and how nature has fine-tuned the redox properties of its many intricate molecular machines. Redox reactions often involve transition metal ions and in the group we are investigating the properties, structure and bonding of transition-metal centres in both biological and synthetic molecular machines.
Many redox reactions proceed via radical intermediates and these are, perhaps luckily, often located in mechanistically key locations. In the lab, we use electron paramagnetic resonance (EPR) spectroscopy as a powerful method for obtaining detailed information on the structure and bonding these ubiquitous spin centres. Electrochemistry on the other hand, in particular film electrochemistry, provides insight into the reactions carried out by molecular machines. These (bio)physical methods are supplemented by biochemical and synthetic methods.
I completed my DPhil at the University of Oxford in 2012 under the supervision of Prof. Fraser Armstrong FRS, working primarily on hydrogenases and on understanding how these enzymes are such exceptionally good H2 producers/oxidisers, even in the presence of oxygen. After a one-year PostDoc in the same group, followed by maternity leave, I started my independent career at the School of Biological and Chemical Sciences at Queen Mary University of London in 2013 and was promoted to senior lecturer in 2018. Following another maternity (shared parental) leave, I moved to Imperial College in April 2019.
et al., 2019, Defining optimal electron transfer partners for light-driven cytochrome P450 reactions, Metabolic Engineering, Vol:55, ISSN:1096-7176, Pages:33-43
et al., 2019, Rotaxane-based transition metal complexes: Effect of the mechanical bond on structure and electronic properties, Journal of the American Chemical Society, Vol:141, ISSN:0002-7863, Pages:879-889
et al., Protein film electrochemical EPR spectroscopy as a technique to investigate redox reactions in biomolecules, Chemical Communications, ISSN:1359-7345
et al., 2018, Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control, Bmc Biology, Vol:16, ISSN:1741-7007
et al., 2018, X- ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [ 4Fe-4S] cluster+, Chemical Communications, Vol:54, ISSN:1359-7345, Pages:7175-7178