ortho and para chromophores of green fluorescent protein: controlling electron emission and internal conversion.
ortho and para chromophores of green fluorescent protein: controlling electron emission and internal conversion.
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DOI：
10.1039/c6sc03833f
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发表时间：
2017-02-01
期刊：
影响因子：
8.4
通讯作者：
Fielding HH
中科院分区：
文献类型：
--
作者：
McLaughlin C;Assmann M;Parkes MA;Woodhouse JL;Lewin R;Hailes HC;Worth GA;Fielding HH
绿色荧光蛋白（GFP）作为一种高效的荧光探针和光诱导电子供体，在生物和生化科学中发挥着重要作用。绿色荧光蛋白（GFP）作为一种高效的荧光探针在生物和生化科学中继续发挥重要作用，并且还已知其经历光诱导的氧化还原转化。在这里，我们采用光电子能谱和量子化学计算，以探讨如何酚部分控制电子发射和内部转换之间的竞争，在孤立的GFP发色团阴离子，在400-230 nm范围内的紫外光激发。我们发现，移动的酚基团从帕拉邻位增强内部转换回地面电子状态，但添加一个额外的OH基团的帕拉发色团，在邻位，阻碍内部转换。在量子化学计算的指导下，我们将这些观察结果解释为C-C-C桥周围的扭转被静电排斥增强或被氢键七元环的形成所阻碍。我们还发现，移动的酚基团从帕拉到邻位的分离过程中所需的能量减少，而添加一个额外的OH基团的帕拉发色团在邻位的分离过程中所需的能量增加。这些结果具有潜在的应用在调谐光诱导的氧化还原过程中，这种生物学和技术上重要的荧光蛋白。
Green fluorescent protein (GFP) plays an important role in the biological and biochemical sciences as an efficient fluorescent probe and as a light-induced electron donor. Green fluorescent protein (GFP) continues to play an important role in the biological and biochemical sciences as an efficient fluorescent probe and is also known to undergo light-induced redox transformations. Here, we employ photoelectron spectroscopy and quantum chemistry calculations to investigate how the phenoxide moiety controls the competition between electron emission and internal conversion in the isolated GFP chromophore anion, following photoexcitation with ultraviolet light in the range 400–230 nm. We find that moving the phenoxide group from the para position to the ortho position enhances internal conversion back to the ground electronic state but that adding an additional OH group to the para chromophore, at the ortho position, impedes internal conversion. Guided by quantum chemistry calculations, we interpret these observations in terms of torsions around the C–C–C bridge being enhanced by electrostatic repulsions or impeded by the formation of a hydrogen-bonded seven-membered ring. We also find that moving the phenoxide group from the para position to the ortho position reduces the energy required for detachment processes, whereas adding an additional OH group to the para chromophore at the ortho position increases the energy required for detachment processes. These results have potential applications in tuning light-induced redox processes of this biologically and technologically important fluorescent protein.
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影响因子：
15
作者：
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通讯作者：
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影响因子：
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