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来自海洋光异养细菌希氏玫瑰杆菌的一种三血红素细胞色素相关RC-LH1复合物的冷冻电镜分析

Cryo-EM Analysis of a Tri-Heme Cytochrome-Associated RC-LH1 Complex from the Marine Photoheterotrophic Bacterium Dinoroseobacter Shibae.

作者信息

Wang Weiwei, Liu Yanting, Gu Jiayi, An Shaoya, Ma Cheng, Gao Haichun, Jiao Nianzhi, Shen Jian-Ren, Beatty John Thomas, Koblížek Michal, Zhang Xing, Zheng Qiang, Chen Jing-Hua

机构信息

College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, China.

State Key Laboratory of Marine Environmental Science, College of Ocean and Earth Sciences, Xiamen University, Xiamen, Fujian, 361005, China.

出版信息

Adv Sci (Weinh). 2025 May;12(18):e2413456. doi: 10.1002/advs.202413456. Epub 2025 Mar 20.

DOI:10.1002/advs.202413456
PMID:40112203
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12079452/
Abstract

The reaction center-light harvesting 1 (RC-LH1) complex converts solar energy into electrical energy, driving the initiation of photosynthesis. The authors present a cryo-electron microscopy structure of the RC-LH1 isolated from a marine photoheterotrophic bacterium Dinoroseobacter shibae. The RC comprises four subunits, including a three-heme cytochrome (Cyt) c protein, and is surrounded by a closed LH ring composed of 17 pairs of antenna subunits. Notably, a novel subunit with an N-terminal "helix-turn-helix" motif embedded in the gap between the RC and the LH ring is identified. The purified RC-LH1 complex exhibits high stability in solutions containing Mg or Ca. The periplasmic Cyt c is predicted to bind at the junction between the Cyt subunit and the membrane plane, enabling electron transfer from Cyt c to the proximal heme of the tri-heme Cyt, and subsequently to the special pair of bacteriochlorophylls. These findings provide structural insights into the efficient energy and electron transfer processes within a distinct type of RC-LH1, and shed light on evolutionary adaptations of photosynthesis.

摘要

反应中心-光捕获1(RC-LH1)复合体将太阳能转化为电能,驱动光合作用的启动。作者展示了从海洋光异养细菌希氏玫瑰杆菌中分离出的RC-LH1的冷冻电子显微镜结构。RC由四个亚基组成,包括一个含三个血红素的细胞色素(Cyt)c蛋白,并被一个由17对天线亚基组成的封闭LH环包围。值得注意的是,在RC和LH环之间的间隙中发现了一个具有N端“螺旋-转角-螺旋”基序的新亚基。纯化的RC-LH1复合体在含有镁或钙的溶液中表现出高稳定性。预测周质Cyt c结合在Cyt亚基与膜平面的交界处,使电子从Cyt c转移到三血红素Cyt的近端血红素,随后转移到特殊的一对细菌叶绿素。这些发现为一种独特类型的RC-LH1内高效的能量和电子转移过程提供了结构见解,并揭示了光合作用的进化适应性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/c8c809153f34/ADVS-12-2413456-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/b054d7da4d23/ADVS-12-2413456-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/2eb82abd6075/ADVS-12-2413456-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/e2a75978fbc9/ADVS-12-2413456-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/add840cf2d61/ADVS-12-2413456-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/5855ec48bf6d/ADVS-12-2413456-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/c8c809153f34/ADVS-12-2413456-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/b054d7da4d23/ADVS-12-2413456-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/2eb82abd6075/ADVS-12-2413456-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/e2a75978fbc9/ADVS-12-2413456-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/add840cf2d61/ADVS-12-2413456-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/5855ec48bf6d/ADVS-12-2413456-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/faae/12079452/c8c809153f34/ADVS-12-2413456-g004.jpg

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本文引用的文献

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Unravelling the Roles of Integral Polypeptides in Excitation Energy Transfer of Photosynthetic RC-LH1 Supercomplexes.解析整合多肽在光合 RC-LH1 超复合体激发能传递中的作用。
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Structural diversity and modularity of photosynthetic RC-LH1 complexes.光合作用 RC-LH1 复合物的结构多样性和模块性。
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