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光合光捕获蛋白的光保护构象动力学。

Photoprotective conformational dynamics of photosynthetic light-harvesting proteins.

机构信息

Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.

Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.

出版信息

Biochim Biophys Acta Bioenerg. 2022 Apr 1;1863(4):148543. doi: 10.1016/j.bbabio.2022.148543. Epub 2022 Feb 21.

DOI:10.1016/j.bbabio.2022.148543
PMID:35202576
Abstract

Under high light conditions, excess energy can damage the machinery of oxygenic photosynthesis. Plants have evolved a series of photoprotective processes, including conformational changes of the light-harvesting complexes that activate dissipation of energy as heat. In this mini-review, we will summarize our recent work developing and applying single-molecule methods to investigate the conformational states of the light-harvesting complexes. Through these measurements, we identified dissipative conformations and how they depend on conditions that mimic high light. Our studies revealed an equilibrium between the light-harvesting and dissipative conformations, and that the nature of the equilibrium varies with cellular environment, between proteins, and between species. Finally, we conclude with an outlook on open questions and implications for photosynthetic yields.

摘要

在强光条件下,多余的能量会损害产氧光合作用的机器。植物已经进化出一系列光保护过程,包括光捕获复合物的构象变化,从而激活能量以热量的形式耗散。在这篇迷你综述中,我们将总结我们最近开发和应用单分子方法来研究光捕获复合物构象状态的工作。通过这些测量,我们确定了耗散构象以及它们如何依赖于模拟高光的条件。我们的研究揭示了光捕获和耗散构象之间的平衡,并且该平衡的性质因细胞环境、蛋白质之间和物种之间而异。最后,我们对开放问题和对光合产量的影响进行了展望。

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1
Photoprotective conformational dynamics of photosynthetic light-harvesting proteins.光合光捕获蛋白的光保护构象动力学。
Biochim Biophys Acta Bioenerg. 2022 Apr 1;1863(4):148543. doi: 10.1016/j.bbabio.2022.148543. Epub 2022 Feb 21.
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Single-molecule spectroscopy of LHCSR1 protein dynamics identifies two distinct states responsible for multi-timescale photosynthetic photoprotection.LHCSR1 蛋白动力学的单分子光谱学鉴定出两种负责多时间尺度光合作用光保护的不同状态。
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