Evidence map›Paper›PMID 19429705›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Menaquinone as pool quinone in a purple bacterium.

Barbara Schoepp-Cothenet, Clément Lieutaud, Frauke Baymann, André Verméglio, Thorsten Friedrich, David M Kramer, Wolfgang Nitschke

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

56 citing papers in PubMed, 127 citations in OpenAlex.

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  13. Biosynthesis, Deficiency, and Supplementation of Coenzyme Q.Antioxidants (Basel, Switzerland) · 2023
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  15. Cellular Stress-Induced Metabolites inJournal of natural products · 2022
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  18. Review
  19. The missing enzymatic link in syntrophic methane formation from fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

7 authors at 4 institutions in 3 countries.

Barbara Schoepp-CothenetLaboratoire de Bioénergétique et Ingénierie des Protéines, Unité Propre de Recherche 9036, Institut Fédératif de Recherche 88, Centre National de la Recherche Scientifique, F-13402 Marseille Cedex 20, France. schoepp@ifr88.cnrs-mrs.fr
Clément Lieutaud
Frauke Baymann
André Verméglio
Thorsten Friedrich
David M Kramer
Wolfgang Nitschke
Bioénergétique et Ingénierie des Protéines · FRCentre National de la Recherche Scientifique · FRUniversity of Freiburg · DEWashington State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Purple bacteria have thus far been considered to operate light-driven cyclic electron transfer chains containing ubiquinone (UQ) as liposoluble electron and proton carrier. We show that in the purple gamma-proteobacterium Halorhodospira halophila, menaquinone-8 (MK-8) is the dominant quinone component and that it operates in the Q(B)-site of the photosynthetic reaction center (RC). The redox potentials of the photooxidized pigment in the RC and of the Rieske center of the bc(1) complex are significantly lower (E(m) = +270 mV and +110 mV, respectively) than those determined in other purple bacteria but resemble those determined for species containing MK as pool quinone. These results demonstrate that the photosynthetic cycle in H. halophila is based on MK and not on UQ. This finding together with the unusual organization of genes coding for the bc(1) complex in H. halophila suggests a specific scenario for the evolutionary transition of bioenergetic chains from the low-potential menaquinones to higher-potential UQ in the proteobacterial phylum, most probably induced by rising levels of dioxygen 2.5 billion years ago. This transition appears to necessarily proceed through bioenergetic ambivalence of the respective organisms, that is, to work both on MK- and on UQ-pools. The establishment of the corresponding low- and high-potential chains was accompanied by duplication and redox optimization of the bc(1) complex or at least of its crucial subunit oxidizing quinols from the pool, the Rieske protein. Evolutionary driving forces rationalizing the empirically observed redox tuning of the chain to the quinone pool are discussed.

Indexed as

Amino Acid SequenceCytochrome P-450 Enzyme SystemGenome, BacterialMolecular Sequence DataPhosphorusPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsProtein BindingProteobacteriaQuinonesSequence AlignmentVitamin KCytochrome P-450 Enzyme SystemPhosphorusPhotosynthetic Reaction Center Complex ProteinsQuinonesVitamin K

Identifiers

PMID19429705
PMCPMC2688977
OpenAlexW2009471543

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.