Callis, P.R. (1997) 1La and 1Lb transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins. Methods in Enzymology, 278, 113-150. doi:10.1016/S0076-6879(97)78009-1

has been cited by the following article:

• TITLE: Fluorescence quenching of tryptophan and tryptophanyl dipeptides in solution

  AUTHORS: Aaron P. Osysko, Pedro L. Muíño

  KEYWORDS: Tryptophan; Fluorescence; Quenching; Electron Transfer

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.2 No.3, August 11, 2011

  ABSTRACT: We report measurements of fluorescence quantum yields of tryptophan, tryptophanylaspartate and tryptophanylarginine in several solvents as well as in aqueous solutions over a wide range of pH. We aim to test a computational model developed by Callis and coworkers of fluorescence quantum yield, which postulates that quenching in tryptophan arises from energy loss due to an electron transfer from the aromatic system of tryptophan to one of the amides in the protein backbone. Since the electron transfer state is expected to be high in energy, normally this would not be a possible outcome, but because of its large dipole, such a state should be more accessible in polar solvents. In addition, conditions of low (high) pH, which result in a net positive (negative) charge for the terminal amine (carboxyl) should result in an increase (decrease) of electron transfer rates and low (high) quantum yields. The observed results confirm the predictions of the model.