Evidence map›Paper›PMID 34843002›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2022

Characterisation of the redox centers of ethylbenzene dehydrogenase.

Corina Hagel, Bärbel Blaum, Thorsten Friedrich, Johann Heider

Open access · hybridAbstract read
In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 62% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Article
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

4 authors at 2 institutions in 1 country.

Corina HagelLabor für Mikrobielle Biochemie and Synmikro Zentrum für Synthetische Mikrobiologie, Philipps Universität Marburg, 35043, Marburg, Germany.
Bärbel BlaumInstitut für Biochemie, Albert-Ludwigs Universität, Albertstr. 21, 79104, Freiburg im Breisgau, Germany.ORCID 0000-0003-4312-8912
Thorsten FriedrichInstitut für Biochemie, Albert-Ludwigs Universität, Albertstr. 21, 79104, Freiburg im Breisgau, Germany. friedrich@bio.chemie.uni-freiburg.de.ORCID 0000-0002-0813-7883
Johann HeiderLabor für Mikrobielle Biochemie and Synmikro Zentrum für Synthetische Mikrobiologie, Philipps Universität Marburg, 35043, Marburg, Germany. heider@biologie.uni-marburg.de.ORCID 0000-0001-8328-9716
Philipps University of Marburg · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ethylbenzene dehydrogenase (EbDH), the initial enzyme of anaerobic ethylbenzene degradation from the beta-proteobacterium Aromatoleum aromaticum, is a soluble periplasmic molybdenum enzyme consisting of three subunits. It contains a Mo-bis-molybdopterin guanine dinucleotide (Mo-bis-MGD) cofactor and an 4Fe-4S cluster (FS0) in the α-subunit, three 4Fe-4S clusters (FS1 to FS3) and a 3Fe-4S cluster (FS4) in the β-subunit and a heme b cofactor in the γ-subunit. Ethylbenzene is hydroxylated by a water molecule in an oxygen-independent manner at the Mo-bis-MGD cofactor, which is reduced from the Mo

Indexed as

Iron-Sulfur ProteinsElectron Spin Resonance SpectroscopyMolybdenumOxidation-ReductionOxidoreductasesethylbenzene dehydrogenaseIron-Sulfur ProteinsMolybdenumOxidoreductasesElectron paramagnetic resonanceEthylbenzene dehydrogenaseHeme bIron–sulfur clusterMolybdenum cofactorRedox potential

Identifiers

PMID34843002
PMCPMC8840923
OpenAlexW3214933062

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.