Evidence map›Paper›PMID 39900604›Full record

ArticleScientific reports2025

Actinorhodopsin: an efficient and robust light-driven proton pump for bionanotechnological applications.

Nooraldeen Ayoub, Nadia Djabeur, Daniel Harder, Jean-Marc Jeckelmann, Zöhre Ucurum, Stephan Hirschi, Dimitrios Fotiadis

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Opsins are Phospholipid Scramblases in All Domains of Life.bioRxiv : the preprint server for biology · 2025
    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

7 authors.

Nooraldeen AyoubInstitute of Biochemistry and Molecular Medicine, University of Bern, CH-3012, Bern, Switzerland.
Nadia DjabeurInstitute of Biochemistry and Molecular Medicine, University of Bern, CH-3012, Bern, Switzerland.
Daniel HarderInstitute of Biochemistry and Molecular Medicine, University of Bern, CH-3012, Bern, Switzerland.
Jean-Marc JeckelmannInstitute of Biochemistry and Molecular Medicine, University of Bern, CH-3012, Bern, Switzerland.
Zöhre UcurumInstitute of Biochemistry and Molecular Medicine, University of Bern, CH-3012, Bern, Switzerland.
Stephan HirschiInstitute of Biochemistry and Molecular Medicine, University of Bern, CH-3012, Bern, Switzerland.
Dimitrios FotiadisInstitute of Biochemistry and Molecular Medicine, University of Bern, CH-3012, Bern, Switzerland. dimitrios.fotiadis@unibe.ch.

Funding

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung 205608University of Bern N/A
6 · The paper itself

Abstract

Actinorhodopsins are encoded by a distinct group of microbial rhodopsin (MR) genes predominant in non-marine actinobacteria. Despite their role in the global energy cycle and potential for bionanotechnological applications, our understanding of actinorhodopsin proteins is limited. Here, we characterized the actinorhodopsin RlActR from the freshwater actinobacterium Rhodoluna lacicola, which conserves amino acid residues critical for light-driven proton pumping found in MRs. RlActR was efficiently overexpressed in Escherichia coli in milligram amounts and isolated with high purity and homogeneity. The purified RlActR absorbed green light and its primary proton acceptor exhibited a mildly acidic apparent pK

Indexed as

ActinobacteriaBacterial ProteinsLightProton PumpsRhodopsins, MicrobialCryoelectron MicroscopyEscherichia coliBacterial ProteinsProton PumpsRhodopsins, Microbial

Identifiers

PMID39900604
PMCPMC11790970

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.