title: Backbone modification of retinal induces protein-like excited state dynamics in solution.
abstract: The drastically different reactivity of the retinal chromophore in solution compared to the protein environment is poorly understood. Here, we show that the addition of a methyl group to the C═C backbone of all-trans retinal protonated Schiff base accelerates the electronic decay in solution making it comparable to the proton pump bacteriorhodopsin. Contrary to the notion that reaction speed and efficiency are linked, we observe a concomitant 50% reduction in the isomerization yield. Our results demonstrate that minimal synthetic engineering of potential energy surfaces based on theoretical predictions can induce drastic changes in electronic dynamics toward those observed in an evolution-optimized protein pocket.
authors.affiliation: Department of Chemistry, Chemistry Research Laboratory, University of Oxford, UK.
authors.forename: Tina
authors.initials: T
authors.lastname: Sovdat
authors.forename: Giovanni
authors.initials: G
authors.lastname: Bassolino
authors.forename: Matz
authors.initials: M
authors.lastname: Liebel
authors.forename: Christoph
authors.initials: C
authors.lastname: Schnedermann
authors.forename: Stephen P
authors.initials: SP
authors.lastname: Fletcher
authors.forename: Philipp
authors.initials: P
authors.lastname: Kukura
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry*; D001436:Bacteriorhodopsins / Q000737:chemistry*; D004583:Electrons; D019617:Halobacterium salinarum / Q000737:chemistry*; D007536:Isomerism; D056004:Molecular Dynamics Simulation; D011522:Protons; D012172:Retinaldehyde / Q000737:chemistry*; D012545:Schiff Bases / Q000737:chemistry*
chemical_list: D019843:Archaeal Proteins; D011522:Protons; D012545:Schiff Bases; D001436:Bacteriorhodopsins; D012172:Retinaldehyde