Resonance Raman spectroscopy of sensory rhodopsin II from Natronobacterium pharaonis
Resonance Raman spectroscopy of sensory rhodopsin II from Natronobacterium pharaonis
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DOI：
10.1016/s0014-5793(00)01472-1
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发表时间：
2000-04-28
期刊：
影响因子：
3.5
通讯作者：
Hildebrandt, P
中科院分区：
文献类型：
--
作者：
Gellini, C;Lüttenberg, B;Hildebrandt, P
感觉视紫红质 II (pSRII) 是来自法老嗜盐杆菌的避光受体，已使用旋转细胞技术通过时间分辨共振拉曼 (RR) 光谱进行了研究。在低激光功率激发下，RR光谱很大程度上反映了母体陈旧的pSRII（500），而激光功率的增加导致了对RR光谱有贡献的长寿命中间体的大量积累，所有RR光谱都可以根据C = C拉伸频率之间的相关性，根据分配给母体状态pSRII（500）和长寿命中间体M-400、N-485和O-535的四个分量光谱来一致地进行分析母体状态和中间体 N-485 和 O-535 表现出质子化席夫碱。 C=N 伸缩频率和 MID 同位素位移表明 pSRII(500) 和 O-535 中席夫碱的氢键相互作用很强，而 N-485 (C) 2000 欧洲生化学会联合会中这些相互作用很可能很弱。
Sensory rhodopsin II (pSRII), the photophobic receptor from Natronobacterium pharaonis, has been studied by time-resolved resonance Raman (RR) spectroscopy using the rotating cell technique. Upon excitation with low laser power, the RR spectra largely reflect the parent stale pSRII(500) whereas an increase of the laser power leads to a substantial accumulation of long-lived intermediates contributing to the RR spectra, All RR spectra could consistently be analysed in terms of four component spectra which were assigned to the parent state pSRII(500) and the long-lived intermediates M-400, N-485 and O-535 based on the correlation between the C=C stretching frequency and the absorption maximum, The parent state and the intermediates N-485 and O-535 exhibit a protonated Schiff base. The C=N stretching frequencies and the MID isotopic shifts indicate strong hydrogen bonding interactions of the Schiff base in pSRII(500) and O-535 whereas these interactions are most likely vera weak in N-485 (C) 2000 Federation of European Biochemical Societies.