James M Baxter, Christopher D M Hutchison, Karim Maghlaoui, Violeta Cordon-Preciado, R Marc L Morgan, Pierre Aller, Agata Butryn, Danny Axford, Sam Horrell, Robin L Owen, Selina L S Storm, Nicholas E Devenish, Jasper J van Thor
The chromophores of reversibly switchable fluorescent proteins (rsFPs) undergo photoisomerization of both the trans and cis forms. Concurrent with cis/trans photoisomerisation, rsFPs typically become protonated on the phenolic oxygen resulting in a blue shift of the absorption. A synthetic rsFP referred to as rsEospa, derived from EosFP family, displays the same spectroscopic behavior as the GFP-like rsFP Dronpa at pH 8.4 and involves the photoconversion between nonfluorescent neutral and fluorescent anionic chromophore states...
November 3, 2022: Journal of Physical Chemistry. B