Thesis subject: Capturing divergent catalytic mechanisms in two dioxygenases using time-resolved crystallography and spectrosocpy

Two structurally related metallo-enzymes accept the same substrate, but produce distinct products. These enzymes play important roles in glycopeptide antibiotics biosynthesis and are implicated in human metabolic diseases. Improving our understanding of their mechanisms, may lead to development of new pharmaceutical strategies.

Specifically, this project investigates how structural dynamics electronic states of the catalytic metal ion affect divergence in product formation. These intermediates are found in many biological processes, but remain difficult to study.

This project uses a combination of time-resolved serial crystallography and X-ray spectroscopies; X-ray emission- (XES) and X-ray absorption spectroscopy (XAS). This research will make use of cutting-edge synchrotron techniques such as the new flagship beamline ID29 and ID26.