Elucidation of mechanisms of energy dissipation in proteins by time- and space-resolved observation

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。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。在这项研究中，我们观察到的振动能量迁移的细胞色素b562和肌红蛋白通过使用反斯托克斯UVRR光谱和阐明的距离依赖性的振动能量迁移。

Excess energy generated in an active site in proteins transferred to and dissipates in the protein moiety. 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 observed the vibrational energy migration in cytochrome b562 and myoglobin by using anti-Stokes UVRR spectroscopy and elucidated distance dependence of the vibrational energy migration.