Resonance Raman study of the primary photochemistry of bacteriorhodopsin.
Resonance Raman study of the primary photochemistry of bacteriorhodopsin.
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细菌视紫红质初级光化学的共振拉曼研究。
DOI：
10.1073/pnas.78.12.7379
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发表时间：
1981
影响因子：
11.1
通讯作者：
Ebrey,TG
中科院分区：
文献类型：
--
作者：
Pande,J;Callender,RH;Ebrey,TG
在液氮温度下获得了细菌视紫红质的光适应形式bRLA 568及其第一个光产物K628的共振拉曼多组分光谱。用已知的样品组成，在我们的辐照条件下，用计算机差减技术，可以得到bRLA 568和K628的光谱。与以前的结果一致，我们发现bRLA 568和K628都含有通过视黄醇的质子化席夫碱与脱辅基蛋白连接的发色团。无论是颜料形式，悬浮在水或2 H2O，比较密切的光谱特征的全反式和13-顺式质子化和氘代模型发色团，分别。数据与其他结果一致，表明发色团异构化发生在bRLA 568-K628光跃迁。然而，原位发色团的确切结构似乎不涉及溶液中发现的简单的反式至13-顺式结构。
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.