Evidence map›Paper›PMID 16537491›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Insights into excited-state and isomerization dynamics of bacteriorhodopsin from ultrafast transient UV absorption.

S Schenkl, F van Mourik, N Friedman, M Sheves, R Schlesinger, S Haacke, M Chergui

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

13 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Vibrational coherence transfer in the ultrafast intersystem crossing of a diplatinum complex in solution.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Light-Activated Reversible Imine Isomerization: Towards a Photochromic Protein Switch.Chembiochem : a European journal of chemical biology · 2016
    Article
  6. Article
  7. Review
  8. Article
  9. Aborted double bicycle-pedal isomerization with hydrogen bond breaking is the primary event of bacteriorhodopsin proton pumping.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  10. Control of retinal isomerization in bacteriorhodopsin in the high-intensity regime.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  11. Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  12. Terahertz radiation from bacteriorhodopsin reveals correlated primary electron and proton transfer processes.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  13. Computational photochemistry of retinal proteins.Journal of computer-aided molecular design
    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

7 authors at 3 institutions in 3 countries.

S SchenklLaboratoire de Spectroscopie Ultrarapide, Institut des Sciences et Ingeniérie Chimiques, Faculté des Sciences de Base, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne-Dorigny, Switzerland.
F van Mourik
N Friedman
M Sheves
R Schlesinger
S Haacke
M Chergui
École Polytechnique Fédérale de Lausanne · CHWeizmann Institute of Science · ILForschungszentrum Jülich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A visible-pump/UV-probe transient absorption is used to characterize the ultrafast dynamics of bacteriorhodopsin with 80-fs time resolution. We identify three spectral components in the 265- to 310-nm region, related to the all-trans retinal, tryptophan (Trp)-86 and the isomerized photoproduct, allowing us to map the dynamics from reactants to products, along with the response of Trp amino acids. The signal of the photoproduct appears with a time delay of approximately 250 fs and is characterized by a steep rise ( approximately 150 fs), followed by additional rise and decay components, with time scales characteristic of the J intermediate. The delayed onset and the steep rise point to an impulsive formation of a transition state on the way to isomerization. We argue that this impulsive formation results from a splitting of a wave packet of torsional modes on the potential surface at the branching between the all-trans and the cis forms. Parallel to these dynamics, the signal caused by Trp response rises in approximately 200 fs, because of the translocation of charge along the conjugate chain, and possible mechanisms are presented, which trigger isomerization.

Indexed as

BacteriorhodopsinsBiophysical PhenomenaBiophysicsHalobacterium salinarumIsomerismKineticsMutagenesis, Site-DirectedSpectrophotometry, UltravioletThermodynamicsTryptophanBacteriorhodopsinsTryptophan

Identifiers

PMID16537491
PMCPMC1449653
OpenAlexW1983085323

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.