Evidence map›Paper›PMID 38907135›Full record

ArticlePhotosynthesis research2024

Light harvesting in purple bacteria does not rely on resonance fine-tuning in peripheral antenna complexes.

Erika Keil, Heiko Lokstein, Richard Cogdell, Jürgen Hauer, Donatas Zigmantas, Erling Thyrhaug

Abstract read
In one paragraph

Article in Photosynthesis research, 2024. 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

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

1 citing paper in PubMed.

  1. 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.

Erika KeilTUM School of Natural Sciences, Department of Chemistry, Technical University of Munich, Lichtenbergstrasse 4, 85748, Garching, Germany.
Heiko LoksteinDepartment of Chemical Physics and Optics, Faculty of Mathematics and Physics, Charles University, Ke Karlovu 3, 121 16, Prague, Czech Republic.
Richard CogdellInstitute of Molecular, Cell and Systems Biology, University of Glasgow, Room 402 Davidson Building, Glasgow, G12 8QQ, Scotland.
Jürgen HauerTUM School of Natural Sciences, Department of Chemistry and Catalysis Research Center, Technical University of Munich, Lichtenbergstrasse 4, 85748, Garching, Germany.
Donatas ZigmantasChemical Physics, Lund University, Naturvetarvägen 16, 22362, Lund, Sweden.
Erling ThyrhaugTUM School of Natural Sciences, Department of Chemistry and Catalysis Research Center, Technical University of Munich, Lichtenbergstrasse 4, 85748, Garching, Germany. erling.thyrhaug@tum.de.

Funding

Deutsche Forschungsgemeinschaft 514636421Laser Lab Europe LLC002760Vetenskapsrådet 2021-05836
6 · The paper itself

Abstract

The ring-like peripheral light-harvesting complex 2 (LH2) expressed by many phototrophic purple bacteria is a popular model system in biological light-harvesting research due to its robustness, small size, and known crystal structure. Furthermore, the availability of structural variants with distinct electronic structures and optical properties has made this group of light harvesters an attractive testing ground for studies of structure-function relationships in biological systems. LH2 is one of several pigment-protein complexes for which a link between functionality and effects such as excitonic coherence and vibronic coupling has been proposed. While a direct connection has not yet been demonstrated, many such interactions are highly sensitive to resonance conditions, and a dependence of intra-complex dynamics on detailed electronic structure might be expected. To gauge the sensitivity of energy-level structure and relaxation dynamics to naturally occurring structural changes, we compare the photo-induced dynamics in two structurally distinct LH2 variants. Using polarization-controlled 2D electronic spectroscopy at cryogenic temperatures, we directly access information on dynamic and static disorder in the complexes. The simultaneous optimal spectral and temporal resolution of these experiments further allows us to characterize the ultrafast energy relaxation, including exciton transport within the complexes. Despite the variations in PPC molecular structure manifesting as clear differences in electronic structure and disorder, the energy-transport and-relaxation dynamics remain remarkably similar. This indicates that the light-harvesting functionality of purple bacteria within a single LH2 complex is highly robust to structural perturbations and likely does not rely on finely tuned electronic- or electron-vibrational resonance conditions.

Indexed as

Light-Harvesting Protein ComplexesBacterial ProteinsEnergy TransferLightRhodopseudomonasBacterial ProteinsLight-Harvesting Protein ComplexesEnergy transferExcitonsLight-harvestingUltrafast spectroscopy

Identifiers

PMID38907135
PMCPMC11324704

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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.