Callum first studied Chemistry, Medicinal and Biological Chemistry at the University of York for four years, where he received a first-class honours MSc. The degree composed of core chemistry material such as physical, inorganic and organic chemistry modules, but with additional courses in chemical biology and biochemistry. His final year of the degree involved the analysis of the mechanistic action of a Lytic Polysaccharide MonoOxygenase (LPMO) under the supervision of Prof. Paul Walton. Using techniques such as UV/Vis absorption spectroscopy and Density Functional Theory (DFT), they sought out to understand how the Copper Metal centre redox state changed throughout activity.
They are analyzing the mechanistic action of bacterial and eukaryotic Flavin dependent Monooxygenases (FMOs) through examining its structural features. What key residues are important for the mode of action? They aim to isolate and observe the reactive and key unseen (hydro)peroxy flavin intermediate that oxidizes the substrate. Additionally, they want to probe the NAD(P)H cofactor that reduces and activates the flavin moiety as its mode of action may be more complicated than previously thought. Moreover, through a technique known as Ancestral Protein Reconstruction (APR), structural characterization of ancestral eukaryotic FMOs may provide insight into what residues govern their differing substrate specificities. This research provides further understanding on unseen FMOs and the function of NAD(P)H.
European Summit of Industrial Biotechnology 2017: “ESIB – the new European communication platform for industrial biotechnology”, 14-16 Nov 2017, Graz, Austria.
AIC International School 2017: “Bridging the gap between cryo-EM and crystallography”, 3-6 September 2017, Pavia, Italy.
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