Time‐Resolved Studies of Energy Transfer in Thin Films of Green and Red Fluorescent Proteins

Biologically derived fluorescent proteins are attractive candidates for lasing and sensing due to their excellent optical properties, including their high quantum yield, spectral tunability, and robustness against concentration quenching. Here, a time‐resolved study of the fluorescence dynamics of protein thin films is reported for the enhanced green fluorescent protein (EGFP), the red‐emitting tandem‐dimer protein tdTomato, and blends of EGFP and tdTomato. The exciton dynamics are characterized by using spectrally and time‐resolved measurements of fluorescence and a threefold reduction in lifetime is observed when going from solution to thin film, down to 1 and 0.6 ns for EGFP and tdTomato, respectively. This finding is attributed to a dipole–dipole nonradiative Förster resonant energy transfer (FRET) in solid state. The temporal characteristics of FRET in blended thin films are also studied and increased nonradiative transfer rates are found. Finally, efficient sensitization of a semiconductor surface with a protein thin film is reported. Such a configuration may have important implications for energy harvesting in hybrid organic–inorganic solar cells and other hybrid optoelectronic devices.