Evidence map›Paper›PMID 36369284›Full record

ArticleNature communications2022

Protein control of photochemistry and transient intermediates in phytochromes.

Giacomo Salvadori, Veronica Macaluso, Giulia Pellicci, Lorenzo Cupellini, Giovanni Granucci, Benedetta Mennucci

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
7.1field-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

15 citing papers in PubMed, 37 citations in OpenAlex.

  1. Atomistic simulations reveal the photoactivation mechanism of a carotenoid-binding photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 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

6 authors at 1 institution in 1 country.

Giacomo SalvadoriDepartment of Chemistry and Industrial Chemistry, University of Pisa, Via G. Moruzzi 13, 56126, Pisa, Italy. giacomo.salvadori@phd.unipi.it.
Veronica MacalusoDepartment of Chemistry and Industrial Chemistry, University of Pisa, Via G. Moruzzi 13, 56126, Pisa, Italy.
Giulia PellicciDepartment of Chemistry and Industrial Chemistry, University of Pisa, Via G. Moruzzi 13, 56126, Pisa, Italy.ORCID 0000-0001-5550-6787
Lorenzo CupelliniDepartment of Chemistry and Industrial Chemistry, University of Pisa, Via G. Moruzzi 13, 56126, Pisa, Italy.ORCID 0000-0003-0848-2908
Giovanni GranucciDepartment of Chemistry and Industrial Chemistry, University of Pisa, Via G. Moruzzi 13, 56126, Pisa, Italy.ORCID 0000-0002-4753-6318
Benedetta MennucciDepartment of Chemistry and Industrial Chemistry, University of Pisa, Via G. Moruzzi 13, 56126, Pisa, Italy. benedetta.mennucci@unipi.it.ORCID 0000-0002-4394-0129
University of Pisa · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytochromes are ubiquitous photoreceptors responsible for sensing light in plants, fungi and bacteria. Their photoactivation is initiated by the photoisomerization of the embedded chromophore, triggering large conformational changes in the protein. Despite numerous experimental and computational studies, the role of chromophore-protein interactions in controlling the mechanism and timescale of the process remains elusive. Here, we combine nonadiabatic surface hopping trajectories and adiabatic molecular dynamics simulations to reveal the molecular details of such control for the Deinococcus radiodurans bacteriophytochrome. Our simulations reveal that chromophore photoisomerization proceeds through a hula-twist mechanism whose kinetics is mainly determined by the hydrogen bond of the chromophore with a close-by histidine. The resulting photoproduct relaxes to an early intermediate stabilized by a tyrosine, and finally evolves into a late intermediate, featuring a more disordered binding pocket and a weakening of the aspartate-to-arginine salt-bridge interaction, whose cleavage is essential to interconvert the phytochrome to the active state.

Indexed as

DeinococcusPhytochromeBacterial ProteinsHydrogen BondingKineticsPhotochemistryBacterial ProteinsPhytochrome

Identifiers

PMID36369284
PMCPMC9652276
OpenAlexW4309181478

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.