In the 20th century, X-ray crystallography revealed a molecular world at a level previously unimaginable, far beyond the limits of the microscope. In my research group, we use structural biology techniques including but not limited to X-ray and neutron crystallography, and X-ray free electron laser to understand the mechanisms of metalloenzymes. X-ray crystallography is a powerful tool that gives three dimensional structures at atomic resolution; however, it only provides static pictures. Enzyme reactions are dynamic processes that take place in ultrafast time scale, necessitating the development of new tools and techniques to observe them.
The ultimate goal is to routinely produce “a molecular movie” through time-resolved crystallography utilising rapidly evolving synchrotrons, XFELs and cryoEM to better understand the structural dynamics of biomolecular catalysis.
One of our main research focuses is to understand the catalytic activity and biological function in heme proteins. Heme is essential for the survival of virtually all living systems and has long been recognised as the prosthetic group of the active site in proteins which play significant roles in catalysis, oxygen transport and electron transfer. These are some of life’s most fundamental processes. Our work on heme peroxidases is in collaboration with Professors Peter Moody (University of Leicester), Emma Raven (University of Bristol) and Dr Jon Warrall (University of Essex).
We also utilise neutron crystallography which has the unique power to visualise hydrogen atoms; essential in studying enzyme mechanisms. We collaborate with scientists at Institut Langevin in Grenoble, France and MLZ in Munich, Germany.