Evidence map›Paper›PMID 42221925›Full record

ArticleACS physical chemistry Au2026

Decarboxylation via a Higher Electronic Excited State Drives LSSmOrange Photoconversion.

Hyang Sook Seol, Fangjia Luo, Elke De Zitter, Nipawan Nuemket, Eduard Fron, Neil R McFarlane, Leonie De Vrieze, Janko Civic, Michiel Postelmans, Savannah Van Bel and 19 more

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Article in ACS physical chemistry Au, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

29 authors.

Hyang Sook SeolLaboratory of Biomolecular Network Dynamics, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G bus 2403, Leuven 3001, Belgium.
Fangjia LuoJapan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Japan.ORCID https://orcid.org/0000-0003-0631-6236
Elke De ZitterUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble 38000, France.ORCID https://orcid.org/0000-0001-6325-7354
Nipawan NuemketJapan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Japan.
Eduard FronChem & Tech-Molecular Imaging and Photonics, Department of Chemistry, KU Leuven, Celestijnenlaan 200F bus 2404, Leuven 3001, Belgium.ORCID https://orcid.org/0000-0003-2260-0798
Neil R McFarlaneQuantum Chemistry and Physical Chemistry Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200F bus 2404, Leuven 3001, Belgium.
Leonie De VriezeLaboratory of Biomolecular Network Dynamics, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G bus 2403, Leuven 3001, Belgium.ORCID https://orcid.org/0009-0005-5409-3251
Janko CivicQuantum Chemistry and Physical Chemistry Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200F bus 2404, Leuven 3001, Belgium.ORCID https://orcid.org/0009-0002-9207-835X
Michiel PostelmansLaboratory of Biomolecular Network Dynamics, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G bus 2403, Leuven 3001, Belgium.
Savannah Van BelLaboratory of Biomolecular Network Dynamics, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G bus 2403, Leuven 3001, Belgium.
Shigeki OwadaJapan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Japan.
Kensuke TonoJapan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Japan.
Tomoyuki TanakaSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Toshi ArimaSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Hiroki NoguchiLaboratory of Biomolecular Modelling and Design, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G bus 2403, Leuven 3001, Belgium.
Thi Yen Hang BuiLaboratory of Biomolecular Architecture, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G bus 2403, Leuven 3001, Belgium.
Rie TanakaSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Kazuya HasegawaJapan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Japan.
Kunio HirataSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Dohyun ImDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.ORCID https://orcid.org/0000-0002-6939-7718
Tsuyoshi ArayaDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
Tetsunari KimuraDepartment of Chemistry, Graduate School of Science, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan.
Luc Van MeerveltLaboratory of Biomolecular Architecture, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G bus 2403, Leuven 3001, Belgium.ORCID https://orcid.org/0000-0003-2186-5209
Martin WeikUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble 38000, France.
Jeremy N HarveyQuantum Chemistry and Physical Chemistry Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200F bus 2404, Leuven 3001, Belgium.ORCID https://orcid.org/0000-0002-1728-1596
Jacques-Philippe ColletierUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble 38000, France.ORCID https://orcid.org/0000-0003-1819-4686
So IwataSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Eriko NangoDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
Hideaki MizunoLaboratory of Biomolecular Network Dynamics, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G bus 2403, Leuven 3001, Belgium.ORCID https://orcid.org/0000-0002-6983-5255

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LSSmOrange is a fluorescent protein that exhibits slow photoconversion and is used as an imaging tool to highlight specific subpopulations of molecules. While photoconversion in LSSmOrange is known to involve Kolbe decarboxylation of the E215 side chain, its structural dynamics remain unexplored. We addressed the excited state dynamics of LSSmOrange by using serial femtosecond crystallography (SFX) with an X-ray free electron laser. SFX enabled us to determine the crystal structure of unconverted LSSmOrange without detectable X-ray damage, facilitating a femtosecond optical pumpX-ray probe experiment to track time-resolved structural changes. A decrease in electron density at E215 was observed 250 ps after strong pump laser illumination (mean fluence of 0.31 J/cm

Indexed as

Kolbe decarboxylationphotoswitchable fluorescent proteinstime-resolved serial femtosecond crystallographytime-resolved spectroscopyX-ray free electron laser

Identifiers

PMID42221925
PMCPMC13220194

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