Evidence map›Paper›PMID 29532352›Full record

ArticlePhotosynthesis research2018

Light-driven quinone reduction in heliobacterial membranes.

Trevor S Kashey, Dustin D Luu, John C Cowgill, Patricia L Baker, Kevin E Redding

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Photosynthesis research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  3. Review
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  9. Differential sensitivity to oxygen among the bacteriochlorophylls g in the type-I reaction centers of Heliobacterium modesticaldum.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021
    Article
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  12. Using the Endogenous CRISPR-Cas System ofApplied and environmental microbiology · 2019
    Article
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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

5 authors at 2 institutions in 1 country.

Trevor S KasheySchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, AZ, 85287-1604, USA.
Dustin D LuuSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, AZ, 85287-1604, USA.
John C CowgillSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, AZ, 85287-1604, USA.
Patricia L BakerSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, AZ, 85287-1604, USA.
Kevin E ReddingSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, AZ, 85287-1604, USA. Kevin.Redding@asu.edu.ORCID http://orcid.org/0000-0003-2819-4022
Arizona State University · USUniversity of Wisconsin–Madison · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthetic reaction centers (RCs) evolved > 3 billion years ago and have diverged into Type II RCs reducing quinones and Type I RCs reducing soluble acceptors via iron-sulfur clusters. Photosystem I (PSI), the exemplar Type I RC, uses modified menaquinones as intermediate electron transfer cofactors, but it has been controversial if the Type I RC of heliobacteria (HbRC) uses its two bound menaquinones in the same way. The sequence of the quinone-binding site in PSI is not conserved in the HbRC, and the recently solved crystal structure of the HbRC does not reveal a quinone in the analogous site. We found that illumination of heliobacterial membranes resulted in reduction of menaquinone to menaquinol, suggesting that the HbRC can perform a function thought restricted to Type II RCs. Experiments on membranes and live cells are consistent with the hypothesis that the HbRC preferentially reduces soluble electron acceptors (e.g., ferredoxins) in low light, but switches to reducing lipophilic quinones in high light, when the soluble acceptor pool becomes full. Thus, the HbRC may represent a functional evolutionary intermediate between PSI and the Type II RCs.

Indexed as

BacteriochlorophyllsCell MembraneElectron TransportEubacterialesLightOxidation-ReductionPhotosystem I Protein ComplexQuinonesVitamin K 2BacteriochlorophyllsPhotosystem I Protein ComplexQuinonesVitamin K 2HeliobacteriaQuinoneReaction centersType II reaction centerType I reaction center

Identifiers

PMID29532352
OpenAlexW2791907567

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.