Evidence map›Paper›PMID 25525277›Full record

ArticleThe Journal of biological chemistry2015

Pigment interactions in light-harvesting complex II in different molecular environments.

Parveen Akhtar, Márta Dorogi, Krzysztof Pawlak, László Kovács, Attila Bóta, Teréz Kiss, Győző Garab, Petar H Lambrev

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
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  6. Article
  7. Photoprotective Role of Neoxanthin in Plants and Algae.Molecules (Basel, Switzerland) · 2020
    Review
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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 at 4 institutions in 1 country.

Parveen AkhtarHungarian Academy of Sciences, Biological Research Centre, Temesvári krt. 62, 6726 Szeged and.
Márta DorogiHungarian Academy of Sciences, Biological Research Centre, Temesvári krt. 62, 6726 Szeged and.
Krzysztof PawlakHungarian Academy of Sciences, Biological Research Centre, Temesvári krt. 62, 6726 Szeged and.
László KovácsHungarian Academy of Sciences, Biological Research Centre, Temesvári krt. 62, 6726 Szeged and.
Attila BótaHungarian Academy of Sciences, Research Centre for Natural Sciences, Institute of Materials and Environmental Chemistry, Magyar tudósok körútja 2, 1117 Budapest, Hungary.
Teréz KissHungarian Academy of Sciences, Research Centre for Natural Sciences, Institute of Materials and Environmental Chemistry, Magyar tudósok körútja 2, 1117 Budapest, Hungary.
Győző GarabHungarian Academy of Sciences, Biological Research Centre, Temesvári krt. 62, 6726 Szeged and.
Petar H LambrevHungarian Academy of Sciences, Biological Research Centre, Temesvári krt. 62, 6726 Szeged and. Electronic address: lambrev@brc.hu.
Hungarian Academy of Sciences · HUHUN-REN Research Centre for Natural Sciences · HUHUN-REN Szegedi Biológiai Kutatóközpont · HUInstitute of Materials and Environmental Chemistry · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extraction of plant light-harvesting complex II (LHCII) from the native thylakoid membrane or from aggregates by the use of surfactants brings about significant changes in the excitonic circular dichroism (CD) spectrum and fluorescence quantum yield. To elucidate the cause of these changes, e.g. trimer-trimer contacts or surfactant-induced structural perturbations, we compared the CD spectra and fluorescence kinetics of LHCII aggregates, artificial and native LHCII-lipid membranes, and LHCII solubilized in different detergents or trapped in polymer gel. By this means we were able to identify CD spectral changes specific to LHCII-LHCII interactions, at (-)-437 and (+)-484 nm, and changes specific to the interaction with the detergent n-dodecyl-β-maltoside (β-DM) or membrane lipids, at (+)-447 and (-)-494 nm. The latter change is attributed to the conformational change of the LHCII-bound carotenoid neoxanthin, by analyzing the CD spectra of neoxanthin-deficient plant thylakoid membranes. The neoxanthin-specific band at (-)-494 nm was not pronounced in LHCII in detergent-free gels or solubilized in the α isomer of DM but was present when LHCII was reconstituted in membranes composed of phosphatidylcholine or plant thylakoid lipids, indicating that the conformation of neoxanthin is sensitive to the molecular environment. Neither the aggregation-specific CD bands, nor the surfactant-specific bands were positively associated with the onset of fluorescence quenching, which could be triggered without invoking such spectral changes. Significant quenching was not active in reconstituted LHCII proteoliposomes, whereas a high degree of energetic connectivity, depending on the lipid:protein ratio, in these membranes allows for efficient light harvesting.

Indexed as

Circular DichroismLight-Harvesting Protein ComplexesMembrane LipidsPisum sativumThylakoidsXanthophyllsLight-Harvesting Protein ComplexesMembrane LipidsneoxanthinXanthophyllsCircular Dichroism (CD)Conformational ChangeDetergent SolubilizationFluorescenceMembrane ProteinNon-photochemical QuenchingPhotosynthetic PigmentProtein Aggregation

Identifiers

PMID25525277
PMCPMC4335227
OpenAlexW2083587547

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.