Evidence map›Paper›PMID 38225270›Full record

ArticleNature chemistry2024

Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography.

Andrea Cellini, Madan Kumar Shankar, Amke Nimmrich, Leigh Anna Hunt, Leonardo Monrroy, Jennifer Mutisya, Antonia Furrer, Emma V Beale, Melissa Carrillo, Tek Narsingh Malla and 16 more

Open access · hybridAbstract read
In one paragraph

Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
15.0field-weighted citation impact, top 1% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  11. Transitioning enzyme catalysis towards photocatalysis.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025
    Review
  12. Article
  13. Review
  14. A snapshot love story: what serial crystallography has done and will do for us.Acta crystallographica. Section D, Structural biology · 2024
    Review
  15. Article
  16. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
  17. Illuminating genome repair by photolyase.Photochemistry and photobiology
    Article
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

26 authors at 7 institutions in 4 countries.

Andrea CelliniDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.ORCID 0000-0001-5348-4158
Madan Kumar ShankarDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.ORCID 0000-0002-7944-1081
Amke NimmrichDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.ORCID 0000-0003-0425-2101
Leigh Anna HuntDepartment of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.ORCID 0000-0002-7681-3599
Leonardo MonrroyDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.ORCID 0000-0001-8852-9424
Jennifer MutisyaDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Antonia FurrerPaul Scherrer Institut, Villigen, Switzerland.
Emma V BealePaul Scherrer Institut, Villigen, Switzerland.ORCID 0000-0002-7814-734X
Melissa CarrilloPaul Scherrer Institut, Villigen, Switzerland.ORCID 0000-0002-0744-4486
Tek Narsingh MallaPhysics Department, University of Wisconsin-Milwaukee, Milwaukee, WI, USA.ORCID 0000-0002-1387-0801
Piotr MajDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.ORCID 0000-0002-9832-2344
Lidija VrhovacDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.ORCID 0000-0002-2445-3472
Florian DworkowskiPaul Scherrer Institut, Villigen, Switzerland.ORCID 0000-0001-5004-8684
Claudio CirelliPaul Scherrer Institut, Villigen, Switzerland.ORCID 0000-0003-4576-3805
Philip J M JohnsonPaul Scherrer Institut, Villigen, Switzerland.ORCID 0000-0002-7251-4815
Dmitry OzerovPaul Scherrer Institut, Villigen, Switzerland.ORCID 0000-0002-3274-1124
Emina A StojkovićDepartment of Biology, Northeastern Illinois University, Chicago, IL, USA.ORCID 0000-0002-4971-5213
Leif HammarströmDepartment of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.ORCID 0000-0002-9933-9084
Camila BacellarPaul Scherrer Institut, Villigen, Switzerland.ORCID 0000-0003-2166-241X
Jörg StandfussPaul Scherrer Institut, Villigen, Switzerland.ORCID 0000-0001-8825-386X
Michał MajDepartment of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.ORCID 0000-0003-1567-9514
Marius SchmidtPhysics Department, University of Wisconsin-Milwaukee, Milwaukee, WI, USA.ORCID 0000-0002-0962-9468
Tobias WeinertPaul Scherrer Institut, Villigen, Switzerland.ORCID 0000-0002-0339-3722
Janne A IhalainenDepartment of Biological and Environmental Sciences, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland.ORCID 0000-0002-8741-1587
Weixiao Yuan WahlgrenDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Sebastian WestenhoffDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden. sebastian.westenhoff@kemi.uu.se.ORCID 0000-0002-6961-8015
Paul Scherrer Institute · CHUppsala University · SEUniversity of Gothenburg · SEUniversity of Wisconsin–Milwaukee · USNortheastern Illinois University · USUniversity of Jyväskylä · FIUniversity of Washington · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Charge-transfer reactions in proteins are important for life, such as in photolyases which repair DNA, but the role of structural dynamics remains unclear. Here, using femtosecond X-ray crystallography, we report the structural changes that take place while electrons transfer along a chain of four conserved tryptophans in the Drosophila melanogaster (6-4) photolyase. At femto- and picosecond delays, photoreduction of the flavin by the first tryptophan causes directed structural responses at a key asparagine, at a conserved salt bridge, and by rearrangements of nearby water molecules. We detect charge-induced structural changes close to the second tryptophan from 1 ps to 20 ps, identifying a nearby methionine as an active participant in the redox chain, and from 20 ps around the fourth tryptophan. The photolyase undergoes highly directed and carefully timed adaptations of its structure. This questions the validity of the linear solvent response approximation in Marcus theory and indicates that evolution has optimized fast protein fluctuations for optimal charge transfer.

Indexed as

Deoxyribodipyrimidine Photo-LyaseAnimalsCrystallography, X-RayDrosophila melanogasterElectronsElectron TransportEscherichia coliHumansTryptophanDeoxyribodipyrimidine Photo-LyaseTryptophan

Identifiers

PMID38225270
PMCPMC10997514
OpenAlexW4390880654

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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.