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x region, which is much weaker for purpurin 2 compared to dyad 1.
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note
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2 = 1.08).
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22
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0011746455
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The wavelength-dependent behavior of the ∼1.4 ps component has only a small effect on the shape of the time-dependent fluorescence spectra, reconstructed after normalization of the isotropic kinetics to the steady-state fluorescence spectrum (Figure 3). There is no shift in the emission maximum between 0.3 and 4.3 ps and only a small (∼1 nm) decrease in the bandwidth. We assign the 1.4 ps time constant to cooling of the vibrationally hot purpurin molecules, which are produced following ultrafast (< 100 fs) relaxation from higher vibronic or electronic levels.
-
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25
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Similar results were obtained at other wavelengths, with the anisotropy decaying from 0.40 to 0.012 with a lifetime of 61 fs at 688 nm and from 0.40 to 0.033 in 49 fs at 712 nm.
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26
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note
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1 excited-state absorption, which has a tail extending at least as far as 730 nm (see Figure 7). The kinetics of dyad 1 display no slow rise component after subtraction of the decay kinetics of carotenoid 3 at 701 nm scaled by 26%. Instead, a recovery component of ∼1.2 ps is revealed.
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