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低温电子显微镜和飞秒光谱研究为 CpcL-藻胆体中的能量转移提供了机制见解。

Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes.

机构信息

School of Life Sciences, Peking University, Beijing, 100871, China.

State Key Laboratory of Membrane Biology, Peking University, Beijing, 100871, China.

出版信息

Nat Commun. 2023 Jul 5;14(1):3961. doi: 10.1038/s41467-023-39689-7.

Abstract

Phycobilisomes (PBS) are the major light harvesting complexes of photosynthesis in the cyanobacteria and red algae. CpcL-PBS is a type of small PBS in cyanobacteria that transfers energy directly to photosystem I without the core structure. Here we report the cryo-EM structure of the CpcL-PBS from the cyanobacterium Synechocystis sp. PCC 6803 at 2.6-Å resolution. The structure shows the CpcD domain of ferredoxin: NADP oxidoreductase is located at the distal end of CpcL-PBS, responsible for its attachment to PBS. With the evidence of ultrafast transient absorption and fluorescence spectroscopy, the roles of individual bilins in energy transfer are revealed. The bilin β located near photosystem I has an enhanced planarity and is the red-bilin responsible for the direct energy transfer to photosystem I.

摘要

藻胆体(PBS)是蓝藻和红藻光合作用中的主要光收集复合物。CpcL-PBS 是蓝藻中的一种小型 PBS,它直接将能量传递给光系统 I,而无需核心结构。在这里,我们报告了来自集胞藻 PCC 6803 的 CpcL-PBS 的 cryo-EM 结构,分辨率为 2.6 Å。该结构显示,铁氧还蛋白:NADP 氧化还原酶的 CpcD 结构域位于 CpcL-PBS 的远端,负责其与 PBS 的连接。根据超快瞬态吸收和荧光光谱的证据,揭示了单个类胡萝卜素在能量转移中的作用。位于光系统 I 附近的类胡萝卜素 β 具有增强的平面性,是负责直接将能量转移到光系统 I 的红色类胡萝卜素。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f808/10322944/24c811f9c7f7/41467_2023_39689_Fig1_HTML.jpg

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