Evidence map›Paper›PMID 35307890›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022

Deciphering the Spectral Tuning Mechanism in Proteorhodopsin: The Dominant Role of Electrostatics Instead of Chromophore Geometry.

Jonathan R Church, Gil S Amoyal, Veniamin A Borin, Suliman Adam, Jógvan Magnus Haugaard Olsen, Igor Schapiro

Open access · hybridAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 29% 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

9 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.Journal of the American Chemical Society · 2025
    Article
  3. Article
  4. Ultrafast terahertz Stark spectroscopy reveals the excited-state dipole moments of retinal in bacteriorhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. 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
  7. Article
  8. Article
  9. Review
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 2 institutions in 2 countries.

Jonathan R ChurchFritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.ORCID http://orcid.org/0000-0001-5986-1305
Gil S AmoyalFritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.ORCID http://orcid.org/0000-0002-2505-4692
Veniamin A BorinFritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.ORCID http://orcid.org/0000-0001-7832-1443
Suliman AdamFritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.ORCID http://orcid.org/0000-0002-0891-5008
Jógvan Magnus Haugaard OlsenDTU Chemistry, Technical University of Denmark, DK-2800, Kongens Lyngby, Denmark.ORCID http://orcid.org/0000-0001-7487-944X
Igor SchapiroFritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.ORCID http://orcid.org/0000-0001-8536-6869
Hebrew University of Jerusalem · ILTechnical University of Denmark · DK

Funding

DFG Collaborative Research Centre 1078 221545957H2020 European Research Council 678169Villum Fonden 29478
6 · The paper itself

Abstract

Proteorhodopsin (PR) is a photoactive proton pump found in marine bacteria. There are two phenotypes of PR exhibiting an environmental adaptation to the ocean's depth which tunes their maximum absorption: blue-absorbing proteorhodopsin (BPR) and green-absorbing proteorhodopsin (GPR). This blue/green color-shift is controlled by a glutamine to leucine substitution at position 105 which accounts for a 20 nm shift. Typically, spectral tuning in rhodopsins is rationalized by the external point charge model but the Q105L mutation is charge neutral. To study this tuning mechanism, we employed the hybrid QM/MM method with sampling from molecular dynamics. Our results reveal that the positive partial charge of glutamine near the C

Indexed as

GlutamineRhodopsins, MicrobialLeucineRhodopsinStatic ElectricityGlutamineLeucineproteorhodopsinRhodopsinRhodopsins, MicrobialproteorhodopsinQM/MMretinalrhodopsinspectral tuning

Identifiers

PMID35307890
PMCPMC9325082
OpenAlexW4220920026

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.