What is it about?
The green fluorescent protein chromophore is structurally flexible, making it non-fluorescent and unable to release the proton upon light irradiation. We restored the proton-releasing capability, hence making it a photoacid, through halogen substitutions and structural rigidification. Using ultrafast spectroscopy, we demonstrated that the structural flexibility significantly affects the proton transfer process in terms of rate and solvation.
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Why is it important?
Our findings show how the structural flexibility of a photoacid could affect the excited-state proton transfer process. This can guide the chromophore design in many functional systems that require the photo-triggered proton release.
Read the Original
This page is a summary of: Ultrafast excited-state proton transfer dynamics in dihalogenated non-fluorescent and fluorescent GFP chromophores, The Journal of Chemical Physics, January 2020, American Institute of Physics,
DOI: 10.1063/1.5138666.
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