| Abstract: | Abstract The excitation of the eosin-human serum albumin complex has been investigated with spectral and photochemical techniques. Measurements of the changes in absorption and fluorescence spectra induced by complexing have shown that the first eosin molecule is held more strongly than the next few and that multiple binding leads to an enhanced fluorescence self-quenching. Flash photolytic measurements indicate that dye-dye quenching interactions enhance triplet eosin formation, and that oxygen quenching of the triplet is suppressed when the dye is singly bound. The quantum yield for aerobic photobleaching of the complex has been measured and is interpreted in terms of these findings. |
