Mechanistic insights into lytic polysaccharide monooxygenases: an integrated structure/spectroscopy study

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Metal-containing enzymes perform critical biochemical functions across the full breadth of biology. They are also found in many everyday products such as washing powders and cleaning products. Furthermore, these types of enzymes are used very widely by industry (e.g. paper manufacture). Therefore, any insight we can gain into their detailed biochemistry and chemistry has significant societal benefits. In most of these enzymes the metal ion is an essential feature of the enzyme's active site, and in many cases the metal(s) at the active site is/are (a) transition metals, e.g. Fe, Mn, Cu. What is distinctive about such types of active site is that they are often capable of 'extraordinary' chemistry in which the conversion of normally unreactive substrates is catalysed. This is perhaps no truer than in the enzymes which Nature deploys to convert abundant biomass (e.g. wood, cellulose and methane respectively) through to bio-valuable products, where metal-containing enzymes carry out many of the key conversion steps. As such, knowledge of and utilisation of these enzymes is essential for myriad industries, perhaps the most conspicuous of which is the nascent second-generation biofuel industry in which recalcitrant and abundant biomass is converted through to bioethanol through enzymatic degradation of the biomass feedstock. Indeed this projects concentrates on a brand new set of enzymes called lytic polysaccharide monooxygenase which contain copper. These enzymes are proving to be key factors in our ability to convert waste plant matter (e.g. leaves and stalks) through to biofuel. In fact, these enzymes are part of the reason why several new biorefineries have opened-up around the world which are able to convert grasses through to bioethanol. This project, therefore, seeks to understand in detail how the enzymes work and also to find ways to improve their conversion capabilities.