Abstract
Site-selective fluorescence spectroscopy has been performed for Zn-substituted myoglobin in the lowest optical absorption band at 4 K. The single-site fluorescence spectrum as well as the distribution of the zero-phonon transition energy have been obtained. Furthermore, the density of states of vibrational modes of myoglobin weighted by the coupling strength between the chromophore and the polypeptide chain has been determined from the analysis of the obtained spectrum. This is the first case in which the weighted density of states of low-frequency vibrational modes has been determined in biological materials without employing any model shape functions. The results are compared with those for dye-doped polymers.
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