Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophore

Omri Tau, Alice Henley, Anton N. Boichenko, Nadezhda N. Kleshchina, River Riley, Bingxing Wang, Danielle Winning, Ross Lewin, Ivan P. Parkin, John M. Ward, Helen C. Hailes, Anastasia V. Bochenkova () and Helen H. Fielding ()
Additional contact information
Omri Tau: University College London
Alice Henley: University College London
Anton N. Boichenko: Lomonosov Moscow State University
Nadezhda N. Kleshchina: Lomonosov Moscow State University
River Riley: University College London
Bingxing Wang: University College London
Danielle Winning: University College London
Ross Lewin: University College London
Ivan P. Parkin: University College London
John M. Ward: Department of Biochemical Engineering, University College London
Helen C. Hailes: University College London
Anastasia V. Bochenkova: Lomonosov Moscow State University
Helen H. Fielding: University College London

Nature Communications, 2022, vol. 13, issue 1, 1-7

Abstract: Abstract Green fluorescent protein (GFP), the most widely used fluorescent protein for in vivo monitoring of biological processes, is known to undergo photooxidation reactions. However, the most fundamental property underpinning photooxidation, the electron detachment energy, has only been measured for the deprotonated GFP chromophore in the gas phase. Here, we use multiphoton ultraviolet photoelectron spectroscopy in a liquid-microjet and high-level quantum chemistry calculations to determine the electron detachment energy of the GFP chromophore in aqueous solution. The aqueous environment is found to raise the detachment energy by around 4 eV compared to the gas phase, similar to calculations of the chromophore in its native protein environment. In most cases, electron detachment is found to occur resonantly through electronically excited states of the chromophore, highlighting their importance in photo-induced electron transfer processes in the condensed phase. Our results suggest that the photooxidation properties of the GFP chromophore in an aqueous environment will be similar to those in the protein.

Date: 2022
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DOI: 10.1038/s41467-022-28155-5

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