The photophysics of the green fluorescent protein is governed by the electronic structure of the chromophore at the heart of its β-barrel protein structure. We present the first two-color, resonance-enhanced, multiphoton ionization spectrum of the isolated neutral chromophore in vacuo with supporting electronic structure calculations. We find the absorption maximum to be 3.65 ± 0.05 eV (340 ± 5 nm), which is blue-shifted by 0.5 eV (55 nm) from the absorption maximum of the protein in its neutral form. Our results show that interactions between the chromophore and the protein have a significant influence on the electronic structure of the neutral chromophore during photoabsorption and provide a benchmark for the rational design of novel chromophores as fluorescent markers or photomanipulators.
|Journal||Journal of Physical Chemistry Letters|
|Early online date||03 Oct 2014|
|Publication status||Published - 16 Oct 2014|
- absorption, ultra-violet, time dependent density functional theory, femtosecond, gas-phase
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High Harmonic Generation and Attosecond Dynamics in Small Organic Molecules and BiomoleculesAuthor: Mulholland, P. P., 2019
Supervisor: Dundas, D. (Supervisor)
Student thesis: Doctoral Thesis › Doctor of PhilosophyFile