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The functional role of protein dynamics in photosynthetic reaction centers investigated by elastic and quasielastic neutron scattering

机译:弹性和准中子散射研究蛋白质动力学在光合反应中心的功能作用

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This short review summarizes our current knowledge about the functional relevance of protein dynamics in photosynthetic reaction centers. In the case of Photosystem II membrane fragments, elastic and quasielastic neutron scattering experiments reveal a dynamical transition at about 240 K corresponding to the activation of picosecond molecular motions. Likewise, a "freezing" of molecular dynamics is observed upon dehydration. Intriguingly, these effects correlate with the pronounced temperature- and hydration-dependence of specific electron transfer steps in Photosystem II indicating that molecular dynamics is an indispensable prerequisite for its function. Thus, electron transfer in Photosystem II appears to be a prototypical example for a dynamics-function correlation. Finally, the laser-neutron pump-probe technique is shown to permit in-situ monitoring of molecular dynamics in specific functional states of a protein in real time.
机译:这次简短的评论总结了我们目前关于蛋白质动态在光合反应中心功能相关性的知识。在光系统II膜片段的情况下,弹性和准中子散射实验显示在约240k的动态转变对应于吡缩秒分子运动的激活。同样地,在脱水时观察到分子动力学的“冷冻”。有趣的是,这些效果与光照II中的特定电子转移步骤的明显温度和水合依赖性相关,表明分子动力学是其功能不可或缺的先决条件。因此,照相系统II中的电子传递似乎是动力学函数相关的原型示例。最后,示出了激光中子泵探针技术,以实时地原位监测特定蛋白质的特定功能状态的分子动力学。

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