Evidence map›Paper›PMID 30072383›Full record

ArticleThe Journal of biological chemistry2018

Roles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavage.

Vera Pfanzagl, Kevin Nys, Marzia Bellei, Hanna Michlits, Georg Mlynek, Gianantonio Battistuzzi, Kristina Djinovic-Carugo, Sabine Van Doorslaer, Paul G Furtmüller, Stefan Hofbauer and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Characterization ofApplied and environmental microbiology · 2024
    Article
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  10. A mutant R70V/E166A of short manganese peroxidase showing MnApplied microbiology and biotechnology · 2023
    Article
  11. Unexpected diversity of dye-decolorizing peroxidases.Biochemistry and biophysics reports · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. DyP-Type Peroxidases: Recent Advances and Perspectives.International journal of molecular sciences · 2021
    Review
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

11 authors at 5 institutions in 3 countries.

Vera PfanzaglFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, 1190 Vienna, Austria.ORCID 0000-0002-9361-8365
Kevin Nysthe Department of Physics, University of Antwerp, 2610 Wilrijk, Belgium.ORCID 0000-0001-6502-9064
Marzia Belleithe Departments of Life Sciences and.
Hanna MichlitsFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
Georg Mlynekthe Department for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria.
Gianantonio BattistuzziChemistry and Geology, University of Modena and Reggio Emilia, via Campi 103, 41125 Modena, Italy, and.
Kristina Djinovic-Carugothe Department for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria.
Sabine Van Doorslaerthe Department of Physics, University of Antwerp, 2610 Wilrijk, Belgium.
Paul G FurtmüllerFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, 1190 Vienna, Austria.ORCID 0000-0002-1199-2469
Stefan HofbauerFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, 1190 Vienna, Austria.ORCID 0000-0003-3375-7715
Christian ObingerFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, 1190 Vienna, Austria, christian.obinger@boku.ac.at.ORCID 0000-0002-7133-3430
BOKU University · ATUniversity of Antwerp · BEUniversity of Modena and Reggio Emilia · ITMax Perutz Labs · ATUniversity of Vienna · AT

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Dye-decolorizing peroxidases (DyPs) represent the most recently classified hydrogen peroxide-dependent heme peroxidase family. Although widely distributed with more than 5000 annotated genes and hailed for their biotechnological potential, detailed biochemical characterization of their reaction mechanism remains limited. Here, we present the high-resolution crystal structures of WT B-class DyP from the pathogenic bacterium

Indexed as

Amino Acid SubstitutionArginineAspartic AcidCatalysisCatalytic DomainCircular DichroismColorColoring AgentsCrystallography, X-RayDimerizationEnzyme StabilityHemeHydrogen-Ion ConcentrationHydrogen PeroxideHydrolysisKlebsiella pneumoniaeArginineAspartic AcidColoring AgentsHemeHydrogen PeroxidePeroxidasesRecombinant ProteinsCompound ICompound IIelectron paramagnetic resonance (EPR)enzyme kineticshemeheme peroxidaseKlebsiella pneumoniaoxoironpre-steady-state kineticssite-directed mutagenesisX-ray crystallography

Identifiers

PMID30072383
PMCPMC6153280
OpenAlexW2885487320

What OpenQuestion holds

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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.