Evidence map›Paper›PMID 29203649›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin.

Victor A Lorenz-Fonfria, Mattia Saita, Tzvetana Lazarova, Ramona Schlesinger, Joachim Heberle

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. O to bR transition in bacteriorhodopsin occurs through a proton hole mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Article
  5. Infrared and NMR Spectroscopic Fingerprints of the Asymmetric HChemphyschem : a European journal of chemical physics and physical chemistry · 2021
    Article
  6. Article
  7. Article
  8. How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer.Journal of the American Chemical Society · 2019
    Article
  9. Article
  10. Article
  11. 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

5 authors at 2 institutions in 2 countries.

Victor A Lorenz-FonfriaExperimental Molecular Biophysics, Department of Physics, Freie Universität Berlin, 14195 Berlin, Germany; victor.lorenz@uv.es.
Mattia SaitaExperimental Molecular Biophysics, Department of Physics, Freie Universität Berlin, 14195 Berlin, Germany.
Tzvetana LazarovaUnitat de Biofísica, Departament de Bioquímica i de Biologia Molecular, Centre d'Estudis en Biofísica, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.
Ramona SchlesingerGenetic Biophysics, Department of Physics, Freie Universität Berlin, 14195 Berlin, Germany.
Joachim HeberleExperimental Molecular Biophysics, Department of Physics, Freie Universität Berlin, 14195 Berlin, Germany.
Freie Universität Berlin · DEUniversitat Autònoma de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Infrared spectroscopy has been used in the past to probe the dynamics of internal proton transfer reactions taking place during the functional mechanism of proteins but has remained mostly silent to protonation changes in the aqueous medium. Here, by selectively monitoring vibrational changes of buffer molecules with a temporal resolution of 6 µs, we have traced proton release and uptake events in the light-driven proton-pump bacteriorhodopsin and correlate these to other molecular processes within the protein. We demonstrate that two distinct chemical entities contribute to the temporal evolution and spectral shape of the continuum band, an unusually broad band extending from 2,300 to well below 1,700 cm

Indexed as

Hydrogen-Ion ConcentrationProtonsBacteriorhodopsinsBuffersCytoplasmKineticsMetabolic Networks and PathwaysModels, MolecularMolecular ConformationProtein BindingSpectroscopy, Fourier Transform InfraredWaterBacteriorhodopsinsBuffersProtonsWatercontinuum bandprotonated water clustersproton releaseproton uptaketime-resolved infrared spectroscopy

Identifiers

PMID29203649
PMCPMC5754764
OpenAlexW2771440809

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.