Evidence map›Paper›PMID 37653340›Full record

ArticleNature plants2023

Cryo-EM structures of LHCII in photo-active and photo-protecting states reveal allosteric regulation of light harvesting and excess energy dissipation.

Meixia Ruan, Hao Li, Ying Zhang, Ruoqi Zhao, Jun Zhang, Yingjie Wang, Jiali Gao, Zhuan Wang, Yumei Wang, Dapeng Sun and 2 more

Abstract read
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In one paragraph

Article in Nature plants, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
6.8field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. LHCSR1 Functions as a Dimmer Switch for Light Harvesting.The journal of physical chemistry letters · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 3 countries.

Meixia Ruan *Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0003-4300-2770
Hao Li *School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China.
Ying ZhangLaboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0003-2527-9397
Ruoqi ZhaoInstitute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, China.
Jun ZhangInstitute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, China.ORCID http://orcid.org/0000-0001-9093-9430
Yingjie WangInstitute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, China.
Jiali GaoSchool of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China. gao@jialigao.org.ORCID http://orcid.org/0000-0003-0106-7154
Zhuan WangLaboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.
Yumei WangLaboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.
Dapeng SunLaboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.
Wei DingLaboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China. dingwei@iphy.ac.cn.ORCID http://orcid.org/0000-0003-4368-8215
Yuxiang WengLaboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China. yxweng@iphy.ac.cn.ORCID http://orcid.org/0000-0003-0423-2266
Institute of Physics · CNShenzhen Bay Laboratory · CNFZU ‒ Institute of Physics of the Academy of Sciences of the Czech Republic · CZPeking University · CNSongshan Lake Materials Laboratory · CNUniversity of Minnesota · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The major light-harvesting complex of photosystem II (LHCII) has a dual regulatory function in a process called non-photochemical quenching to avoid the formation of reactive oxygen. LHCII undergoes reversible conformation transitions to switch between a light-harvesting state for excited-state energy transfer and an energy-quenching state for dissipating excess energy under full sunshine. Here we report cryo-electron microscopy structures of LHCII in membrane nanodiscs, which mimic in vivo LHCII, and in detergent solution at pH 7.8 and 5.4, respectively. We found that, under low pH conditions, the salt bridges at the lumenal side of LHCII are broken, accompanied by the formation of two local α-helices on the lumen side. The formation of α-helices in turn triggers allosterically global protein conformational change, resulting in a smaller crossing angle between transmembrane helices. The fluorescence decay rates corresponding to different conformational states follow the Dexter energy transfer mechanism with a characteristic transition distance of 5.6 Å between Lut1 and Chl612. The experimental observations are consistent with the computed electronic coupling strengths using multistate density function theory.

Indexed as

OxygenThylakoidsAllosteric RegulationCryoelectron MicroscopyEnergy TransferOxygen

Identifiers

PMID37653340
OpenAlexW4386332762

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.