Evidence map›Paper›PMID 22947860›Full record

ArticleBiophysical journal2012

Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.

Joel E Morgan, Ahmet S Vakkasoglu, Janos K Lanyi, Johan Lugtenburg, Robert B Gennis, Akio Maeda

Abstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Buried ionizable networks are an ancient hallmark of G protein-coupled receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  8. Article
  9. Article
  10. 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.

Joel E MorganDepartment of Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York.
Ahmet S VakkasogluCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois.
Janos K LanyiDepartment of Physiology and Biophysics, University of California, Irvine, California.
Johan LugtenburgDepartment of Chemistry, University of Leiden, Leiden, The Netherlands.
Robert B GennisCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois; Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois.
Akio MaedaDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois. Electronic address: akio.maeda@gmail.com.

Funding

PROTEIN/LIPID INTERACTIONSR01HL016101 · NHLBI · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GENNIS, ROBERT B · 1985 to 2015
$6.8M
MECHANISM OF CHLORIDE TRANSPORT BY HALORHODOPSINR01GM029498 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI LANYI, JANOS K · 1985 to 2013
$2.1M
PROTEIN/LIPID INTERACTIONSR37HL016101 · NHLBI · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GENNIS, ROBERT B. · 1993 to 2002
$1.5M
NHLBI NIH HHS HL16101NHLBI NIH HHS R01 HL016101NHLBI NIH HHS R37 HL016101NIGMS NIH HHS 5R01GM029498-31NIGMS NIH HHS R01 GM029498
6 · The paper itself

Abstract

In the photocycle of bacteriorhodopsin at pH 7, a proton is ejected to the extracellular medium during the protonation of Asp-85 upon formation of the M intermediate. The group that releases the ejected proton does not become reprotonated until the prephotolysis state is restored from the N and O intermediates. In contrast, at acidic pH, this proton release group remains protonated to the end of the cycle. Time-resolved Fourier transform infrared measurements obtained at pH 5 and 7 were fitted to obtain spectra of kinetic intermediates, from which the spectra of M and N/O versus unphotolyzed state were calculated. Vibrational features that appear in both M and N/O spectra at pH 7, but not at pH 5, are attributable to deprotonation from the proton release group and resulting structural alterations. Our results agree with the earlier conclusion that this group is a protonated internal water cluster, and provide a stronger experimental basis for this assignment. A decrease in local polarity at the N-C bond of the side chain of Lys-216 resulting from deprotonation of this water cluster may be responsible for the increase in the proton affinity of Asp-85 through M and N/O, which is crucial for maintaining the directionality of proton pumping.

Indexed as

PhotolysisProtonsAspartic AcidBacteriorhodopsinsHydrogen-Ion ConcentrationMutationSpectrum AnalysisAspartic AcidBacteriorhodopsinsProtons

Identifiers

PMID22947860
PMCPMC3414889

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.