Abstract
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.
Original language | English |
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Pages (from-to) | 3588-3592 |
Number of pages | 5 |
Journal | Journal of Physical Chemistry Letters |
Volume | 5 |
Issue number | 20 |
DOIs | |
Publication status | Published - 16 Oct 2014 |
Externally published | Yes |
Keywords
- absorption
- femtosecond
- gas phase
- time-dependent density functional theory
- ultraviolet