Evidence map›Paper›PMID 22496367›Full record

ArticleThe Journal of biological chemistry2012

Rhodanese functions as sulfur supplier for key enzymes in sulfur energy metabolism.

Clément Aussignargues, Marie-Cécile Giuliani, Pascale Infossi, Elisabeth Lojou, Marianne Guiral, Marie-Thérèse Giudici-Orticoni, Marianne Ilbert

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. 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
0.8field-weighted citation impact, top 26% 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, 40 citations in OpenAlex.

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  11. Omics Integration for Mitochondria Systems Biology.Antioxidants & redox signaling · 2020
    Review
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  13. Applied 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

7 authors at 3 institutions in 1 country.

Clément AussignarguesUnité de Bioénergétique et Ingénierie des Protéines, Institut de Microbiologie de la Méditerranée-CNRS, Aix-Marseille University, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
Marie-Cécile Giuliani
Pascale Infossi
Elisabeth Lojou
Marianne Guiral
Marie-Thérèse Giudici-Orticoni
Marianne Ilbert
Centre National de la Recherche Scientifique · FRInstitut de Microbiologie de la Méditerranée · FRAix-Marseille Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

How microorganisms obtain energy is a challenging topic, and there have been numerous studies on the mechanisms involved. Here, we focus on the energy substrate traffic in the hyperthermophilic bacterium Aquifex aeolicus. This bacterium can use insoluble sulfur as an energy substrate and has an intricate sulfur energy metabolism involving several sulfur-reducing and -oxidizing supercomplexes and enzymes. We demonstrate that the cytoplasmic rhodanese SbdP participates in this sulfur energy metabolism. Rhodaneses are a widespread family of proteins known to transfer sulfur atoms. We show that SbdP has also some unusual characteristics compared with other rhodaneses; it can load a long sulfur chain, and it can interact with more than one partner. Its partners (sulfur reductase and sulfur oxygenase reductase) are key enzymes of the sulfur energy metabolism of A. aeolicus and share the capacity to use long sulfur chains as substrate. We demonstrate a positive effect of SbdP, once loaded with sulfur chains, on sulfur reductase activity, most likely by optimizing substrate uptake. Taken together, these results lead us to propose a physiological role for SbdP as a carrier and sulfur chain donor to these key enzymes, therefore enabling channeling of sulfur substrate in the cell as well as greater efficiency of the sulfur energy metabolism of A. aeolicus.

Indexed as

BacteriaBacterial ProteinsCytoplasmEnergy MetabolismSulfurThiosulfate SulfurtransferaseBacterial ProteinsSulfurThiosulfate Sulfurtransferase

Identifiers

PMID22496367
PMCPMC3370178
OpenAlexW2092906222

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.