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

在蛋白质的活性部位产生的多余能量转移到蛋白质部分并在蛋白质部分消散。紫外共振拉曼光谱可以选择性地监测色氨酸、酪氨酸和苯丙氨酸等芳香族氨基酸残基的拉曼光谱。反斯托克斯拉曼强度反映了处于振动激发态的布居。因此，反斯托克斯UVRR强度可以直接探测蛋白质中残基的振动能量。在这项研究中，我们用反斯托克斯UVRR光谱观察了细胞色素b562和肌红蛋白的振动能量迁移，阐明了振动能量迁移的距离依赖性。

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.