Nonisomerizable non-retinal chromophores initiate light-induced conformational alterations in bacterioopsin

被引:23
作者
Aharoni, A
Weiner, L
Lewis, A [1 ]
Ottolenghi, M
Sheves, M
机构
[1] Hebrew Univ Jerusalem, Dept Appl Phys, IL-91904 Rehovot, Israel
[2] Hebrew Univ Jerusalem, Dept Phys Chem, IL-91904 Rehovot, Israel
[3] Weizmann Inst Sci, Dept Organ Chem, IL-76100 Rehovot, Israel
[4] Weizmann Inst Sci, Dept Chem Serv, IL-76100 Rehovot, Israel
关键词
D O I
10.1021/ja004035a
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The photoactivation of retinal proteins is usually interpreted in terms of C=C photoisomerization of the retinal moiety, which triggers appropriate conformational changes in the protein. In this work several dye molecules. characterized by a completely rigid structure in which no double-bond isomerization is possible, were incorporated into the binding site of bacteriorhodopsin (bR). Using a light-induced chemical reaction of a labeled EPR probe, it was observed that specific conformational alterations in the protein are induced following light absorption by the dye molecules occupying the binding site. The exact nature of these changes and their relationship to those occurring in the bR photocycle are still unclear. Nevertheless, their occurrence proves that C=C or C=NH+ isomerization is not a prerequisite for protein conformational changes in a retinal protein. More generally, we show that conformational changes, leading to changes in reactivity, may be induced in proteins by optical excitation of simple nonisomerizable dyes located in the macromolecular matrix.
引用
收藏
页码:6612 / 6616
页数:5
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