Mechanism of resonant electron emission from the deprotonated GFP chromophore and its biomimetics† †Electronic supplementary information (ESI) available: Experimental and computational details, calculated VEEs in anions and radicals, orbitals involved in electronic transitions, detailed discussion of direct and resonant spectral shapes, mechanism of vibrational autodetachment out of S1 above the S1/D0 crossing, impact of the substituents, and coordinates of the optimized structures. See DOI: 10.

By uncovering the mechanism of UV resonant electron emission, we show that the GFP biomimetics are more stable to photooxidation. The Green Fluorescent Protein (GFP), which is widely used in bioimaging, is known to undergo light-induced redox transformations. Electron transfer is thought to occur resonantly through excited states of its chromophore; however, a detailed understanding of the electron gateway states of the chromophore is still missing. Here, we use photoelectron spectroscopy and high-level quantum chemistry calculations to show that following UV excitation, the ultrafast electron dynamics in the chromophore anion proceeds via an excited shape resonance strongly coupled to the open continuum. The impact of this state is found across the entire 355–315 nm excitation range, from above the first bound–bound transition to below the opening of higher-lying continua. By disentangling the electron dynamics in the photodetachment channels, we provide an important reference for the adiabatic position of the electron gateway state, which is located at 348 nm, and discover the source of the curiously large widths of the photoelectron spectra that have been reported in the literature. By introducing chemical modifications to the GFP chromophore, we show that the detachment threshold and the position of the gateway state, and hence the underlying excited-state dynamics, can be changed systematically. This enables a fine tuning of the intrinsic electron emission properties of the GFP chromophore and has significant implications for its function, suggesting that the biomimetic GFP chromophores are more stable to photooxidation.