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A New Strategy to Photoactivate Green Fluorescent Protein
Author(s) -
Groff Dan,
Wang Feng,
Jockusch Steffen,
Turro Nicholas J.,
Schultz Peter G.
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201003797
Subject(s) - fluorophore , fluorescence , green fluorescent protein , chemistry , photochemistry , fluorescence in the life sciences , biophysics , optics , biochemistry , physics , biology , gene
A bright idea : A photoactivatable GFP variant has been developed by mutagenesis of the fluorophore tyrosine to a photocaged o ‐nitrobenzyl tyrosine. This protein is practically nonfluorescent until exposed to 365 nm light, which increases fluorescence nearly 100‐fold. The quenching mechanism as suggested by crystallography and time‐resolved UV/Vis spectroscopy is most likely due to photon‐induced electron transfer to the nitrobenzyl group.