Spatiotemporal mapping of energy dissipation in proteins

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Excess energy generated in an active site in proteins transferred to and dissipates in the protein moiety. No direct observation of the energy migration within protein moiety has not been reported because it is difficult to perform the observation. Ultraviolet resonance Raman (UVRR) spectroscopy can selectively monitor Raman bands of aromatic amino acid residues, such as tryptophan, tyrosine and phenylalanine. Anti-Stokes Raman intensity reflects the population in vibrationally excited states. Therefore, anti-Stokes UVRR intensity can be a direct probe of vibrational energy of residues in a protein. In this study, we succeeded in observing the vibrational energy migration in photoexcited heme proteins by using anti-Stokes UVRR spectroscopy