Solvatochromism of the green fluorescence protein chromophore and its derivatives.
The solvatochromic behavior of the green fluorescence protein (GFP) chromophore (p-hydroxybenzylideneimidazolone, p-HBDI) and its derivatives (p-methoxybenzylideneimidazolone, p-MeOBDI, and N-methyl-p-hydroxybenzylideneimidazolonium iodide, p-HBDIMe+) was studied using UV-vis-absorption spectroscopy in a wide array of solvents. The relative contribution of specific (polarity) vs nonspecific (hydrogen-bonding) solvation to the absorbance spectra was studied. On the basis of these data, we discuss the nature of the absorption peak of the protonated and deprotonated forms of the wild-type GFP.
Dong
Jian
J
School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332-0400, USA.
Solntsev
Kyril M
KM
Tolbert
Laren M
LM
D049452:Green Fluorescent Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D048288:Imidazolines / Q000737:chemistry*; D007700:Kinetics; D011487:Protein Conformation
C502519:4-hydroxybenzylidene-1,2-dimethylimidazolinone; D048288:Imidazolines; D049452:Green Fluorescent Proteins