Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophore
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.
Citations by journals
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Journal of Physical Chemistry Letters
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Journal of Physical Chemistry Letters
3 publications, 30%
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Accounts of Chemical Research
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Accounts of Chemical Research
2 publications, 20%
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Journal of Physical Chemistry A
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Journal of Physical Chemistry A
1 publication, 10%
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Journal of Chemical Theory and Computation
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Journal of Chemical Theory and Computation
1 publication, 10%
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Chemical Science
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Chemical Science
1 publication, 10%
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Journal of Chromatography A
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Journal of Chromatography A
1 publication, 10%
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Citations by publishers
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American Chemical Society (ACS)
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American Chemical Society (ACS)
7 publications, 70%
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Royal Society of Chemistry (RSC)
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Royal Society of Chemistry (RSC)
1 publication, 10%
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Elsevier
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Elsevier
1 publication, 10%
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