An NMR investigation of lytic polysaccharide monooxygenases
Abstract
Bioeconomy requires sustainable sources of biomass (e.g. chitin and cellulose) to use as energy, feed and biomaterials. In the quest of biomass conversion, lytic polysaccharide monooxygenases (LPMOs) are key enzymatic players. To exploit the full potential of LPMOs, a functional and structural understanding is crucial. In this thesis, we have used the unique versatility of nuclear magnetic resonance (NMR) spectroscopy to characterize and better understand key aspects of LPMO functionality; including their structural features, the effect of copper on LPMO structure and substrate interactions, the molecular basis of their substrate binding, the location of the electron transfer event, their dynamic features, and the role of LPMO-associated carbohydrate-binding modules (CBMs).
Has parts
Paper 1: Courtade, Gaston; Wimmer, Reinhard; Kjendseth, Åsmund Røhr; Preims, Marita; Felice, Alfons K.G.; Dimarogona, Maria; Vaaje-Kolstad, Gustav; Sørlie, Morten; Sandgren, Mats; Ludwig, Roland; Eijsink, Vincent; Aachmann, Finn Lillelund. Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America 2016 ;Volum 113.(21) s. 5922-5927 https://doi.org/10.1073/pnas.1602566113Paper 2: Courtade, Gaston; Le, Simone Balzer; Sætrom, Gerd Inger; Brautaset, Trygve; Aachmann, Finn Lillelund. A novel expression system for lytic polysaccharide monooxygenases. Carbohydrate Research 2017 ;Volum 448. s. 212-219 https://doi.org/10.1016/j.carres.2017.02.003
Paper 3: Courtade, Gaston; Forsberg, Zarah; Heggset, Ellinor Bævre; Eijsink, Vincent; Aachmann, Finn Lillelund. The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation. Journal of Biological Chemistry 2018 ;Volum 293.(34) s. 13006-13015 Is not included due to copyright available at https://doi.org/10.1074/jbc.RA118.004269
Paper 4: Courtade, G.*, Ciano, L.*, Forsberg, Z., Sørlie, M, Wimmer, R., Eijsink, V. G. H., Walton, P. H., Aachmann, F. L. (2018) An integrated NMR/EPR spectroscopic study into the substrate-enzyme interactions of a chitin-active lytic polysaccharide monooxgyenase Is not included due to copyright
Paper 5: Courtade, Gaston; Balzer, Simone; Forsberg, Zarah; Vaaje-Kolstad, Gustav; Eijsink, Vincent; Aachmann, Finn Lillelund. 1H, 13C, 15N resonance assignment of the chitin-active lytic polysaccharide monooxygenase BlLPMO10A from Bacillus licheniformis. Biomolecular NMR Assignments 2015 ;Volum 9.(1) s. 207-210 Is not included due to copyright available at https://doi.org/10.1007/s12104-014-9575-x
Paper 6: Courtade, Gaston; Wimmer, Reinhard; Dimarogona, Maria; Sandgren, Mats; Eijsink, Vincent; Aachmann, Finn Lillelund. Backbone and side-chain 1H, 13C, and 15N chemical shift assignments for the apo-form of the lytic polysaccharide monooxygenase NcLPMO9C. Biomolecular NMR Assignments 2016 ;Volum 10.(2) s. 277-280 Is not included due to copyright available at https://doi.org/10.1007/s12104-016-9683-x
Paper 7: Courtade, Gaston; Forsberg, Zarah; Vaaje-Kolstad, Gustav; Eijsink, Vincentius Gerardus Henricus; Aachmann, Finn Lillelund. Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C. Biomolecular NMR Assignments 2017 ;Volum 11.(2) s. 257-264 Is not included due to copyright available at https://doi.org/10.1007/s12104-017-9759-2
Paper 8: Kitaoku, Yoshihito; Courtade, Gaston; Petrovic, Dejan; Fukamizo, Tamo; Eijsink, Vincent; Aachmann, Finn Lillelund. Resonance assignments for the apo-form of the cellulose-active lytic polysaccharide monooxygenase TaLPMO9A. Biomolecular NMR Assignments 2018 ;Volum 12.(2) s. 357-361 Is not included due to copyright available at https://doi.org/10.1007/s12104-018-9839-y