Experimental and theoretical studies into the structural importance of the imine versus the amine function of the histidine brace motif of LPMO’s
(2022) BOSS 2022 — Location: UNamur (4.July.2022)
Files
BOSS_poster_2022_UgoGilbert.pdf
Open Access - Adobe PDF
- 631.85 KB
Details
- Authors
- Abstract
- 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 will be used to generate the most accurate models of the LPMO active site to date. The first one will be based on traditional small molecule models, different structural parameters will be modified across similar compounds such as the chelate ring size, the position and the methylation of the imidazole or the imine versus the amine function. The second approach will be the developing of a new generation of accurate histidine brace mimics using foldamer scaffolds. 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.
- Affiliations
Citations
Gilbert, U., Singleton, M., & Robiette, R. (2022). Experimental and theoretical studies into the structural importance of the imine versus the amine function of the histidine brace motif of LPMO’s. BOSS 2022, UNamur. https://hdl.handle.net/2078.5/104581