Evidence map›Paper›PMID 25708355›Full record

ArticleThe journal of physical chemistry. B2015

Variation of exciton-vibrational coupling in photosystem II core complexes from Thermosynechococcus elongatus as revealed by single-molecule spectroscopy.

Sepideh Skandary, Martin Hussels, Alexander Konrad, Thomas Renger, Frank Müh, Martin Bommer, Athina Zouni, Alfred J Meixner, Marc Brecht

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Structural basis of light-harvesting in the photosystem II core complex.Protein science : a publication of the Protein Society · 2020
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

9 authors.

Sepideh Skandary†IPTC and Lisa+ Center, Universität Tübingen, Tübingen, Germany.
Martin Hussels†IPTC and Lisa+ Center, Universität Tübingen, Tübingen, Germany.
Alexander Konrad†IPTC and Lisa+ Center, Universität Tübingen, Tübingen, Germany.
Thomas Renger‡Institut für Theoretische Physik, Johannes Kepler Universität, Linz, Austria.
Frank Müh‡Institut für Theoretische Physik, Johannes Kepler Universität, Linz, Austria.
Martin Bommer§Institut für Biologie, Humboldt Universität zu Berlin, Berlin, Germany.
Athina Zouni§Institut für Biologie, Humboldt Universität zu Berlin, Berlin, Germany.
Alfred J Meixner†IPTC and Lisa+ Center, Universität Tübingen, Tübingen, Germany.
Marc Brecht†IPTC and Lisa+ Center, Universität Tübingen, Tübingen, Germany.

Funding

Austrian Science Fund FWF P 24774
6 · The paper itself

Abstract

The spectral properties and dynamics of the fluorescence emission of photosystem II core complexes are investigated by single-molecule spectroscopy at 1.6 K. The emission spectra are dominated by sharp zero-phonon lines (ZPLs). The sharp ZPLs are the result of weak to intermediate exciton-vibrational coupling and slow spectral diffusion. For several data sets, it is possible to surpass the effect of spectral diffusion by applying a shifting algorithm. The increased signal-to-noise ratio enables us to determine the exciton-vibrational coupling strength (Huang-Rhys factor) with high precision. The Huang-Rhys factors vary between 0.03 and 0.8. The values of the Huang-Rhys factors show no obvious correlation between coupling strength and wavelength position. From this result, we conclude that electrostatic rather than exchange or dispersive interactions are the main contributors to the exciton-vibrational coupling in this system.

Indexed as

VibrationAlgorithmsDiffusionEnergy TransferModels, MolecularPhotosystem II Protein ComplexProtein ConformationSpectrum AnalysisSynechococcusPhotosystem II Protein Complex

Identifiers

PMID25708355
PMCPMC4368080

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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.