Pande J, Callender R H, Ebrey T G
Proc Natl Acad Sci U S A. 1981 Dec;78(12):7379-82. doi: 10.1073/pnas.78.12.7379.
Resonance Raman multicomponent spectra of the light-adapted form of bacteriorhodopsin, bRLA568, and its first photoproduct, K628, have been obtained at liquid nitrogen temperatures. The spectra of both bRLA568 and K628 could be obtained with the known sample compositions under our irradiating conditions and computer subtraction techniques. In agreement with previous results, we find that both bRLA568 and K628 contain chromophores linked to the apoprotein by protonated Schiff bases of retinal. Neither pigment form, suspended in H2O or 2H2O, compares closely to the spectral features of all-trans and 13-cis protonated and deuterated model chromophores, respectively. The data are consistent with other results, suggesting that a chromophore isomerization takes place in the bRLA568-to-K628 phototransition. However, the exact structure of the in situ chromophore would appear not to involve simple trans-to-13-cis structures found in solution.
在液氮温度下获得了光适应型细菌视紫红质bRLA568及其首个光产物K628的共振拉曼多组分光谱。在我们的辐照条件和计算机减法技术下，利用已知的样品组成可以获得bRLA568和K628的光谱。与之前的结果一致，我们发现bRLA568和K628都含有通过视网膜的质子化席夫碱与脱辅基蛋白相连的发色团。悬浮在H2O或2H2O中的两种色素形式分别与全反式和13-顺式质子化及氘代模型发色团的光谱特征都不太相符。这些数据与其他结果一致，表明在bRLA568到K628的光转变过程中发生了发色团异构化。然而，原位发色团的确切结构似乎并不涉及溶液中发现的简单的反式到13-顺式结构。
