Evidence map›Paper›PMID 26387727›Full record

ArticleScientific reports2015

Proteomics of the organohalide-respiring Epsilonproteobacterium Sulfurospirillum multivorans adapted to tetrachloroethene and other energy substrates.

Tobias Goris, Christian L Schiffmann, Jennifer Gadkari, Torsten Schubert, Jana Seifert, Nico Jehmlich, Martin von Bergen, Gabriele Diekert

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
7.5field-weighted citation impact, top 3% 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

19 citing papers in PubMed, 50 citations in OpenAlex.

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  17. Isolation and Characterization ofFrontiers in microbiology · 2017
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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 3 institutions in 2 countries.

Tobias GorisDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, 07743 Jena, Germany.
Christian L SchiffmannDepartment of Proteomics, Helmholtz Centre for Environmental Research - UFZ, Permoserstr. 15, 04318 Leipzig, Germany.
Jennifer GadkariDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, 07743 Jena, Germany.
Torsten SchubertDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, 07743 Jena, Germany.
Jana SeifertInstitute of Animal Science, Hohenheim University, 70593 Stuttgart, Germany.
Nico JehmlichDepartment of Proteomics, Helmholtz Centre for Environmental Research - UFZ, Permoserstr. 15, 04318 Leipzig, Germany.
Martin von BergenDepartment of Proteomics, Helmholtz Centre for Environmental Research - UFZ, Permoserstr. 15, 04318 Leipzig, Germany.
Gabriele DiekertDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, 07743 Jena, Germany.
Friedrich Schiller University Jena · DEHelmholtz Centre for Environmental Research · DEUniversity of Hohenheim · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Organohalide respiration is an environmentally important but poorly characterized type of anaerobic respiration. We compared the global proteome of the versatile organohalide-respiring Epsilonproteobacterium Sulfurospirillum multivorans grown with different electron acceptors (fumarate, nitrate, or tetrachloroethene [PCE]). The most significant differences in protein abundance were found for gene products of the organohalide respiration region. This genomic region encodes the corrinoid and FeS cluster containing PCE reductive dehalogenase PceA and other proteins putatively involved in PCE metabolism such as those involved in corrinoid biosynthesis. The latter gene products as well as PceA and a putative quinol dehydrogenase were almost exclusively detected in cells grown with PCE. This finding suggests an electron flow from the electron donor such as formate or pyruvate via the quinone pool and a quinol dehydrogenase to PceA and the terminal electron acceptor PCE. Two putative accessory proteins, an IscU-like protein and a peroxidase-like protein, were detected with PCE only and might be involved in PceA maturation. The proteome of cells grown with pyruvate instead of formate as electron donor indicates a route of electrons from reduced ferredoxin via an Epsilonproteobacterial complex I and the quinone pool to PCE.

Indexed as

Bacterial ProteinsEnergy MetabolismEpsilonproteobacteriaFerredoxinsFormatesGene Expression ProfilingNitratesOxidoreductasesOxygen ConsumptionPrincipal Component AnalysisProteomicsPyruvic AcidQuinonesTetrachloroethyleneBacterial ProteinsFerredoxinsFormatesformic acidNitratesOxidoreductasesPyruvic AcidQuinonestetrachloroethene dehalogenasetetrachloroethene reductaseTetrachloroethylene

Identifiers

PMID26387727
PMCPMC4585668
OpenAlexW2469007563

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.