Resonantly Enhanced Multi-Photon Ionization Spectrum of the Neutral Green Fluorescent Protein Chromophore

Jason Greenwood, Jordan Miles, Simone De Camillis, Peter Mulholland, Lijuan Zhang, Michael A. Parkes, Helen C. Hailes, Helen H. Fielding

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16 Citations (Scopus)
252 Downloads (Pure)

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 languageEnglish
Pages (from-to)3588-3592
JournalJournal of Physical Chemistry Letters
Volume5
Early online date03 Oct 2014
DOIs
Publication statusPublished - 16 Oct 2014

Keywords

  • absorption, ultra-violet, time dependent density functional theory, femtosecond, gas-phase

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