...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Physical chemistry chemical physics: PCCP >Protein conformational alterations induced by the retinal excited state in proton and sodium pumping rhodopsins
【24h】

Protein conformational alterations induced by the retinal excited state in proton and sodium pumping rhodopsins

机译：质子和钠泵罗豆蛋白的视网膜激发态诱导蛋白质构象改变

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Retinal proteins' biological activity is triggered by the retinal chromophore's light absorption, which initiates a photocycle. However, the mechanism by which retinal light excitation induces the protein's response is not completely understood. Recently, two new retinal proteins were discovered, namely, King Sejong 1-2 (KS1-2) and Nonlabens (Donghaeana) dokdonensis (DDR2), which exhibit H+ and Na+ pumping activities, respectively. To pinpoint whether protein conformation alterations can be achieved without light-induced retinal C-13=C-14 double-bond isomerization, we utilized the hydroxylamine reaction, which cleaves the protonated Schiff base bond through which the retinal chromophore is covalently bound to the protein. The reaction is accelerated by light even though the cleavage is not a photochemical reaction. Therefore, the cleavage reaction may serve as a tool to detect protein conformation alterations. We discovered that in both KS1-2 and DDR2, the hydroxylamine reaction is light accelerated, even in artificial pigments derived from synthetic retinal in which the crucial C-13=C-14 double-bond isomerization is prevented. Therefore, we propose that in both proteins the light-induced retinal charge redistribution taking place in the retinal excited state polarizes the protein, which, in turn, triggers protein conformation alterations. A further general possible application of the present finding is associated with other photoreceptor proteins having retinal or other non-retinal chromophores whose light excitation may affect the protein conformation.
机译：视网膜蛋白质生物活性是由视网膜发色团的光的吸收，从而启动一个光循环触发。然而，通过该视网膜光激发诱导蛋白的反应机理尚未完全理解。最近，有两个新的视网膜蛋白质被发现，即世宗1-2（KS1-2）和Nonlabens（Donghaeana）dokdonensis（DDR2），它们分别具有H +和Na +抽奖活动。为了查明是否蛋白质构象的改变可以在不光诱导的视网膜C-13 = C-14双键异构化来实现，我们利用的羟胺反应，其切割该质子化的席夫碱键，通过该视网膜发色团共价结合到蛋白。该反应通过光即使切割的是不是一个光化学反应加速。因此，裂解反应可以用作检测蛋白质构象改变的工具。我们发现，在这两个KS1-2和DDR2，羟胺反应加速光，即使在从其中防止关键C-13 = C-14双键异构化合成视黄醛衍生的人工颜料。因此，我们建议，在这两种蛋白质在视网膜激发态光致视网膜电荷再分布正在发生两极分化的蛋白，这反过来又触发蛋白质构象的改变。本发现的另一个一般可能的应用与具有视网膜或其他非视网膜的发色团，其光激发可影响蛋白质的构象其他感光体蛋白有关。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号