Abstract
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. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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Groff, D., Wang, F., Jockusch, S., Turro, N. J., & Schultz, P. G. (2010). A new strategy to photoactivate green fluorescent protein. Angewandte Chemie - International Edition, 49(42), 7677–7679. https://doi.org/10.1002/anie.201003797
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