Evidence map›Paper›PMID 25621306›Full record

ArticleSOJ biochemistry

Low-Temperature Trapping of Photointermediates of the Rhodopsin E181Q Mutant.

Megan N Sandberg, Jordan A Greco, Nicole L Wagner, Tabitha L Amora, Lavoisier A Ramos, Min-Hsuan Chen, Barry E Knox, Robert R Birge

Abstract read
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In one paragraph

Article in SOJ biochemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Ultrafast transient absorption spectra and kinetics of human blue cone visual pigment at room temperature.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. A short story on how chromophore is hydrolyzed from rhodopsin for recycling.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  3. Review
  4. Ultrafast spectra and kinetics of human green-cone visual pigment at room temperature.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Implications of short time scale dynamics on long time processes.Structural dynamics (Melville, N.Y.) · 2017
    Review
  6. 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

8 authors.

Megan N SandbergDepartments of Chemistry and Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
Jordan A GrecoDepartments of Chemistry and Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
Nicole L WagnerDepartments of Chemistry and Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
Tabitha L AmoraDepartments of Chemistry and Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
Lavoisier A RamosDepartments of Chemistry and Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
Min-Hsuan ChenDepartments of Biochemistry and Molecular Biology and Ophthalmology State University of New York Upstate Medical University, Syracuse, NY 13210, USA.
Barry E KnoxDepartments of Biochemistry and Molecular Biology and Ophthalmology State University of New York Upstate Medical University, Syracuse, NY 13210, USA.
Robert R BirgeDepartments of Chemistry and Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.

Funding

STRUCTURE/FUNCTION OF SHORT WAVELENGTH VISUAL PIGMENTSR01EY011256 · NEI · UPSTATE MEDICAL UNIVERSITY · PI KNOX, BARRY E · 1997 to 2011
$2.6M
MOLECULAR MECHANISMS OF PHOTORECEPTOR FUNCTIONR01EY012975 · NEI · UPSTATE MEDICAL UNIVERSITY · PI KNOX, BARRY E · 2000 to 2010
$2.3M
PHOTOPHYSICS OF VISUAL CHROMOPHORES AND RHODOPSINR01GM034548 · NIGMS · UNIVERSITY OF CONNECTICUT STORRS · PI BIRGE, ROBERT RICHARDS · 1985 to 2012
$1.9M
NEI NIH HHS R01 EY011256NEI NIH HHS R01 EY012975NIGMS NIH HHS R01 GM034548
6 · The paper itself

Abstract

Three active-site components in rhodopsin play a key role in the stability and function of the protein: 1) the counter-ion residues which stabilize the protonated Schiff base, 2) water molecules, and 3) the hydrogen-bonding network. The ionizable residue Glu-181, which is involved in an extended hydrogen-bonding network with Ser-186, Tyr-268, Tyr-192, and key water molecules within the active site of rhodopsin, has been shown to be involved in a complex counter-ion switch mechanism with Glu-113 during the photobleaching sequence of the protein. Herein, we examine the photobleaching sequence of the E181Q rhodopsin mutant by using cryogenic UV-visible spectroscopy to further elucidate the role of Glu-181 during photoactivation of the protein. We find that lower temperatures are required to trap the early photostationary states of the E181Q mutant compared to native rhodopsin. Additionally, a Blue Shifted Intermediate (BSI, λ

Indexed as

Absorption spectroscopyBlue-Shifted Intermediate (BSI)E181QGlu-181Low-Temperature trappingPhotobleaching sequencePhotointermediatesRhodopsin

Identifiers

PMID25621306
PMCPMC4301618

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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.