Oxidized flavin cofactors exhibit an even wider range of fluorescence intensities and lifetimes than tryptophan. The source of this quenching is better understood: flavin quenching is almost always by electron transfer from nearby unexcited tryptophan and tyrosine to the excited state of the flavin. The same appears to be the case for many of the fluorescent dyes that are attached to proteins for various imaging and diagnostic purposes. We are modeling the efficiency of this process with the same tools we use for modeling Trp fluorescence.

Publications

Callis PR, Liu T , "Short Range Photoinduced Electron Transfer in Proteins: QM-MM Simulations of Tryptophan and Flavin Fluorescence Quenching in Proteins." Chemi Phys. (2006) in press+A60+A25

Personnel:

Keywords:

Biophysical, Protein Chemistry