Spatiotemporal mapping of energy dissipation in proteins

在蛋白质的活性位点产生的过量能量转移到蛋白质部分并在蛋白质部分中消散。由于难以进行观察，因此尚未报道蛋白质部分内能量迁移的直接观察。紫外共振拉曼（UVRR）光谱可以选择性地监测芳香族氨基酸残基（如色氨酸、酪氨酸和苯丙氨酸）的拉曼谱带。反斯托克斯拉曼强度反映了振动激发态的布居数。因此，反斯托克斯UVRR强度可以是蛋白质中残基振动能的直接探针。在本研究中，我们成功地利用反斯托克斯UVRR光谱观察到光激发血红素蛋白中的振动能量迁移

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