Lytic Polysaccharide Monooxygenases (LPMOs) are recently discovered enzymes which are found in the secretomes of saprophytic organisms. LPMOs are key components in biological biomass degradation insofar as they cause the oxidation scission of glycosidic bonds in polysaccharides, including those found in the most recalcitrant polysaccharides such as crystalline cellulose and chitin. As such, LPMOs significantly boost the action of canonical cellulases and hold much potential for the commercial production of cellulosic bioethanol. This talk will cover the discovery of the copper active site of LPMOs, the discovery and structural/spectroscopic characterisation of new classes of LPMOs (AA11 and AA13), and some of the physico-chemical properties of the active sites of these enzymes. In particular the role of the active site motif known as the histidine brace (figure) will be discussed, showing how it facilitates the activation of O2 at the copper site, which, in turn, then oxidatively attacks the polysaccharide. The details of this mechanism will be discussed in the context of the recent structural determination of AA9 LPMO-polysaccharide complex alongside spectroscopic and DFT studies of the enzyme.

Structure, function and spectroscopy studies of lytic polysaccharide monooxygenases

254th National Meeting (2017)

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