Evidence map›Paper›PMID 30674680›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

One-megadalton metalloenzyme complex in

Simona G Huwiler, Claudia Löffler, Sebastian E L Anselmann, Hans-Joachim Stärk, Martin von Bergen, Jennifer Flechsler, Reinhard Rachel, Matthias Boll

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 44 citations in OpenAlex.

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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 1 country.

Simona G HuwilerDepartment of Microbiology, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany.
Claudia LöfflerDepartment of Microbiology, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany.
Sebastian E L AnselmannDepartment of Microbiology, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany.
Hans-Joachim StärkDepartment of Analytical Chemistry, Helmholtz-Centre for Environmental Research - UFZ, 04318 Leipzig, Germany.
Martin von BergenDepartment of Molecular Systems Biology, Helmholtz-Centre for Environmental Research - UFZ, 04318 Leipzig, Germany.
Jennifer FlechslerCentre for Electron Microscopy/Anatomy, Faculty of Biology & Preclinical Medicine, University of Regensburg, 93040 Regensburg, Germany.
Reinhard RachelCentre for Electron Microscopy/Anatomy, Faculty of Biology & Preclinical Medicine, University of Regensburg, 93040 Regensburg, Germany.ORCID 0000-0001-6367-1221
Matthias BollDepartment of Microbiology, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany; matthias.boll@biologie.uni-freiburg.de.ORCID 0000-0001-8062-8049
University of Freiburg · DEHelmholtz Centre for Environmental Research · DEUniversity of Regensburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversible biological electron transfer usually occurs between redox couples at standard redox potentials ranging from +0.8 to -0.5 V. Dearomatizing benzoyl-CoA reductases (BCRs), key enzymes of the globally relevant microbial degradation of aromatic compounds at anoxic sites, catalyze a biological Birch reduction beyond the negative limit of this redox window. The structurally characterized BamBC subunits of class II BCRs accomplish benzene ring reduction at an active-site tungsten cofactor; however, the mechanism and components involved in the energetic coupling of endergonic benzene ring reduction have remained hypothetical. We present a 1-MDa, membrane-associated, Bam[(BC)

Indexed as

Oxidation-ReductionBenzeneBiological TransportCatalysisDinitrocresolsElectron TransportEnzymesGeobacterMetalloproteinsMetalsMultiprotein ComplexesOxidoreductases Acting on CH-CH Group Donors4,6-dinitro-o-cresolBenzenebenzoyl-coenzyme A reductase (dearomatizing)DinitrocresolsEnzymesMetalloproteinsMetalsMultiprotein ComplexesOxidoreductases Acting on CH-CH Group Donorsaromatic compoundelectron bifurcationelectron transfermembrane protein complexmetalloenzyme

Identifiers

PMID30674680
PMCPMC6369795
OpenAlexW2914358741

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.