Govindjee R, Becher B, Ebrey T G
Biophys J. 1978 Apr;22(1):67-77. doi: 10.1016/S0006-3495(78)85471-X.
The fluorescence from the purple membrane protein (PM) of Halobacterium halobium and its relation to the primary photochemical events have been studied. The emission spectrum at 77 degrees K has structure, with peaks at 680, 710-715, and 730-735 nm. The excitation spectrum shows a single peak centered at 580 nm. This and a comparison of the fluorescence intensity at 77 degrees K under a variety of conditions with the amounts of the bathoproduct (or K, the only photoproduct seen at this temperature) formed suggest that the source of the fluorescence is the purple membrane itself, not the photoproduct. From the difference in several of their properties, we suggest that the fluorescing state of the pigment is different from the excited state which leads to photoconversion.
对嗜盐菌紫膜蛋白(PM)的荧光及其与初级光化学事件的关系进行了研究。77K时的发射光谱具有结构,在680、710 - 715和730 - 735nm处有峰值。激发光谱显示一个以580nm为中心的单峰。这一点以及在各种条件下77K时荧光强度与所形成的副产物(或K,在此温度下唯一可见的光产物)量的比较表明,荧光的来源是紫膜本身,而非光产物。从它们若干性质的差异来看,我们认为色素的荧光状态不同于导致光转化的激发态。