Evidence map›Paper›PMID 18536726›Full record

ArticleNature structural & molecular biology2008

Molecular mechanism of energy conservation in polysulfide respiration.

Mika Jormakka, Ken Yokoyama, Takahiro Yano, Masatada Tamakoshi, Satoru Akimoto, Tatsuro Shimamura, Paul Curmi, So Iwata

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

73 citing papers in PubMed, 160 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Review
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  7. Article
  8. The critical role of a conserved lysine residue in periplasmic nitrate reductase catalyzed reactions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
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  9. Frontiers in microbiology · 2024
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  10. Article
  11. Generation of zero-valent sulfur from dissimilatory sulfate reduction in sulfate-reducing microorganisms.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Transcriptional Control ofApplied and environmental microbiology · 2023
    Article
  13. Frontiers in microbiology · 2023
    Article
  14. Review
  15. An unprecedented function for a tungsten-containing oxidoreductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Bacterial Oxidases of the CytochromeAntioxidants & redox signaling · 2021
    Review

13 more citing papers are in PubMed but not listed here.

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 6 institutions in 3 countries.

Mika JormakkaDepartment of Biophysics, University of New South Wales, Barker Street, Sydney, New South Wales 2052, Australia. m.jormakka@centenary.org.au
Ken Yokoyama
Takahiro Yano
Masatada Tamakoshi
Satoru Akimoto
Tatsuro Shimamura
Paul Curmi
So Iwata
Japan Science and Technology Agency · JPUNSW Sydney · AURIKEN Center for Integrative Medical Sciences · JPSPring-8 · JPTokyo Institute of Technology · JPTokyo University of Pharmacy and Life Sciences · JP

Funding

Wellcome Trust 079209Wellcome Trust 079209/Z/06/Z
6 · The paper itself

Abstract

Bacterial polysulfide reductase (PsrABC) is an integral membrane protein complex responsible for quinone-coupled reduction of polysulfide, a process important in extreme environments such as deep-sea vents and hot springs. We determined the structure of polysulfide reductase from Thermus thermophilus at 2.4-A resolution, revealing how the PsrA subunit recognizes and reduces its unique polyanionic substrate. The integral membrane subunit PsrC was characterized using the natural substrate menaquinone-7 and inhibitors, providing a comprehensive representation of a quinone binding site and revealing the presence of a water-filled cavity connecting the quinone binding site on the periplasmic side to the cytoplasm. These results suggest that polysulfide reductase could be a key energy-conserving enzyme of the T. thermophilus respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane via a previously unknown mechanism.

Indexed as

Energy MetabolismBinding SitesCatalytic DomainCell MembraneDimerizationElectronsElectron TransportModels, MolecularOxidoreductasesProtein Structure, SecondaryProtein SubunitsProtonsQuinonesStatic ElectricitySulfidesThermus thermophilusOxidoreductasespolysulfidepolysulfide reductaseProtein SubunitsProtonsQuinonesSulfides

Identifiers

PMID18536726
PMCPMC2887006
OpenAlexW1967838127

What OpenQuestion holds

Textmetadata
LicenceTDM
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.