Gilbert, Ugo
[UCL]
Singleton, Michael L.
[UCL]
Robiette, Raphaël
[UCL]
Lytic polysaccharide monooxygenases (LPMO) are a family of copper containing metalloenzymes important for biofuel and biochemical production due to their ability to oxidatively cleave the strong glycosidic C-H bonds in cellulose. The active site of LPMO consists of a single copper atom bound in a T-shaped N3 coordination environment called the histidine brace. The same structure is also found in particulate methane monooxygenase suggesting that the histidine brace is responsible for the oxidative capabilities of the enzymes. However, the role of the histidine brace as well as many other structural features of the active site remain unclear. Synthesizing and studying synthetic models of the histidine brace can increase the understanding of the structural features important for reactivity and generate new powerful catalysts for the oxidation of organic substrates. Currently, the limited number of LPMO model complexes that have been described and the large structural variation between these makes comparison difficult, limiting the understanding of how different modifications affect reactivity. In this PhD project, two complimentary approaches, based on small molecule biomimetics and foldamer based scaffolds, will be used to generate the most accurate models of the LPMO active site to date. Through systematic variation of both first and second coordination spheres, we aim to generate well-defined series of complexes that will allow us to develop a structure-reactivity relationship. In doing so, we aim to define the important features necessary in biomimetic copper complexes for the oxidation of C-H bonds with high bond dissociation energies.
Bibliographic reference |
Gilbert, Ugo ; Singleton, Michael L. ; Robiette, Raphaël. Experimental and theoretical studies into the structural importance of the histidine brace motif of LPMO's.MOCS 2021 (UClouvain, 03/12/2021). |
Permanent URL |
http://hdl.handle.net/2078.1/270134 |