Hydrogen bonding properties of Coumarin 151, 500, and 35: the effect of substitution at the 7-amino position

The steady-state spectral properties (absorption and emission) of three structurally similar Coumarin dyes, C151, C500, and C35 were investigated in 13 different solvents. A Kamlet-Taft (KT) analysis of the spectral peak frequencies reveals that, in addition to polarity, hydrogen bonding between the carbonyl oxygen and a protic solvent in the excited state imparts maximum stabilization for C151 and minimum for C35, while that for C500 lies in between. The spectral properties of the three dyes in two solvents, chloroform and THF, which have similar polarity in the KT scale but have only hydrogen-bond donor (chloroform) and hydrogen-bond acceptor (THF) properties, are seen to be sensitive to the substitution pattern at the 7-amino position. In addition, a slow emission spectral relaxation is observed for C151 and C500 having a time constant of approximately 500 ps in chloroform. For C35 this was too fast to be detected by the time resolution of our setup. The exact reason for this slow spectral relaxation in chloroform is unclear at present, and further studies are needed to understand clearly the structural effects on the hydrogen bonding dynamics of these dyes.