Evidence map›Paper›PMID 28094925›Full record

ArticleJournal of the American Chemical Society2017

Retinal-Based Proton Pumping in the Near Infrared.

Srividya Ganapathy, Hanka Venselaar, Que Chen, Huub J M de Groot, Klaas J Hellingwerf, Willem J de Grip

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Merocyanines form bacteriorhodopsins with strongly bathochromic absorption maxima.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024
    Article
  3. Article
  4. Rhodopsin driven microbial COEnvironmental microbiology · 2023
    Article
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  7. Review
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  19. Article
  20. Functional Expression ofFrontiers in bioengineering and biotechnology · 2019
    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

6 authors at 3 institutions in 1 country.

Srividya GanapathyLeiden Institute of Chemistry, Leiden University , 2333 CC Leiden, The Netherlands.ORCID 0000-0003-1264-9387
Hanka VenselaarCentre for Molecular and Biomolecular Informatics, Radboud University Medical Center , 6500 HB Nijmegen, The Netherlands.
Que ChenSwammerdam Institute for Life Sciences, University of Amsterdam , 1090 GE Amsterdam, The Netherlands.
Huub J M de GrootLeiden Institute of Chemistry, Leiden University , 2333 CC Leiden, The Netherlands.
Klaas J HellingwerfSwammerdam Institute for Life Sciences, University of Amsterdam , 1090 GE Amsterdam, The Netherlands.
Willem J de GripLeiden Institute of Chemistry, Leiden University , 2333 CC Leiden, The Netherlands.
Leiden University · NLNetherlands Institute for Neuroscience · NLRadboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteorhodopsin (PR) and Gloeobacter rhodopsin (GR) are retinal-based light-driven proton pumps that absorb visible light (maxima at 520-540 nm). Shifting the action spectra of these proton pumps beyond 700 nm would generate new prospects in optogenetics, membrane sensor technology, and complementation of oxygenic phototrophy. We therefore investigated the effect of red-shifting analogues of retinal, combined with red-shifting mutations, on the spectral properties and pump activity of the resulting pigments. We investigated a variety of analogues, including many novel ones. One of the novel analogues we tested, 3-methylamino-16-nor-1,2,3,4-didehydroretinal (MMAR), produced exciting results. This analogue red-shifted all of the rhodopsin variants tested, accompanied by a strong broadening of the absorbance band, tailing out to 850-950 nm. In particular, MMAR showed a strong synergistic effect with the PR-D212N,F234S double mutant, inducing an astonishing 200 nm red shift in the absorbance maximum. To our knowledge, this is by far the largest red shift reported for any retinal protein. Very importantly, all MMAR-containing holoproteins are the first rhodopsins retaining significant pump activity under near-infrared illumination (730 nm light-emitting diode). Such MMAR-based rhodopsin variants present very promising opportunities for further synthetic biology modification and for a variety of biotechnological and biophysical applications.

Indexed as

Infrared RaysMolecular StructureProton PumpsRetinaldehydeProton PumpsRetinaldehyde

Identifiers

PMID28094925
PMCPMC5342321
OpenAlexW2574116968

What OpenQuestion holds

Textmetadata
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.