Evidence map›Paper›PMID 26669441›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

The terminal phycobilisome emitter, LCM: A light-harvesting pigment with a phytochrome chromophore.

Kun Tang, Wen-Long Ding, Astrid Höppner, Cheng Zhao, Lun Zhang, Yusaku Hontani, John T M Kennis, Wolfgang Gärtner, Hugo Scheer, Ming Zhou and 1 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

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  5. Molecular glue for phycobilisome attachment to photosystem II inProceedings of the National Academy of Sciences of the United States of America · 2025
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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

11 authors.

Kun TangState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; Max Planck Institute for Chemical Energy Conversion, D-45470 Mülheim an der Ruhr, Germany;
Wen-Long DingState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China;
Astrid HöppnerX-Ray Facility and Crystal Farm, Heinrich-Heine-Universität, D-40225 Dusseldorf, Germany;
Cheng ZhaoState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China;
Lun ZhangState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China;
Yusaku HontaniBiophysics Section, Department of Physics and Astronomy, Faculty of Sciences, VU University, De Boelelaan 1081, NL-1081 HV Amsterdam, The Netherlands;
John T M KennisBiophysics Section, Department of Physics and Astronomy, Faculty of Sciences, VU University, De Boelelaan 1081, NL-1081 HV Amsterdam, The Netherlands;
Wolfgang GärtnerMax Planck Institute for Chemical Energy Conversion, D-45470 Mülheim an der Ruhr, Germany;
Hugo ScheerDepartment Biologie I, Universität München, D-80638 Munich, Germany.
Ming ZhouState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China;
Kai-Hong ZhaoState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; khzhao@163.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthesis relies on energy transfer from light-harvesting complexes to reaction centers. Phycobilisomes, the light-harvesting antennas in cyanobacteria and red algae, attach to the membrane via the multidomain core-membrane linker, L(CM). The chromophore domain of L(CM) forms a bottleneck for funneling the harvested energy either productively to reaction centers or, in case of light overload, to quenchers like orange carotenoid protein (OCP) that prevent photodamage. The crystal structure of the solubly modified chromophore domain from Nostoc sp. PCC7120 was resolved at 2.2 Å. Although its protein fold is similar to the protein folds of phycobiliproteins, the phycocyanobilin (PCB) chromophore adopts ZZZssa geometry, which is unknown among phycobiliproteins but characteristic for sensory photoreceptors (phytochromes and cyanobacteriochromes). However, chromophore photoisomerization is inhibited in L(CM) by tight packing. The ZZZssa geometry of the chromophore and π-π stacking with a neighboring Trp account for the functionally relevant extreme spectral red shift of L(CM). Exciton coupling is excluded by the large distance between two PCBs in a homodimer and by preservation of the spectral features in monomers. The structure also indicates a distinct flexibility that could be involved in quenching. The conclusions from the crystal structure are supported by femtosecond transient absorption spectra in solution.

Indexed as

Bacterial ProteinsCrystallography, X-RayEnergy TransferKineticsLightModels, MolecularMutationNostocPhotosynthesisPhycobiliproteinsPhycobilisomesProtein FoldingProtein MultimerizationProtein Structure, TertiarySpectrophotometryBacterial ProteinsPhycobiliproteinsPhycobilisomescore-membrane linkercrystal structurecyanobacteriaphotosynthesisphycobilisome

Identifiers

PMID26669441
PMCPMC4702970

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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.