In Vitro Heme Coordination of a Dye-Decolorizing Peroxidase-The Interplay of Key Amino Acids, pH, Buffer and Glycerol.

Kevin Nys, Vera Pfanzagl, Jeroen Roefs, Christian Obinger, Sabine Van Doorslaer

Open access · goldAbstract readEvaluation Study

In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

0.1field-weighted citation impact, top 56% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 2 institutions in 2 countries.

Kevin NysBIMEF Laboratory, Department of Chemistry, University of Antwerp, 2610 Antwerp, Belgium.ORCID 0000-0001-6502-9064

Vera PfanzaglDivision of Biochemistry, Department of Chemistry, BOKU-University of Natural Resources and Life Sciences, 1190 Vienna, Austria.ORCID 0000-0002-9361-8365

Jeroen RoefsBIMEF Laboratory, Department of Chemistry, University of Antwerp, 2610 Antwerp, Belgium.

Christian ObingerDivision of Biochemistry, Department of Chemistry, BOKU-University of Natural Resources and Life Sciences, 1190 Vienna, Austria.ORCID 0000-0002-7133-3430

Sabine Van DoorslaerBIMEF Laboratory, Department of Chemistry, University of Antwerp, 2610 Antwerp, Belgium.ORCID 0000-0002-1685-9202

University of Antwerp · BEBOKU University · AT

Funding

Research Foundation Flanders / Austrian Science Fund - FWO/FWF lead agency grant G005416N

6 · The paper itself

Abstract

Dye-decolorizing peroxidases (DyPs) have gained interest for their ability to oxidize anthraquinone-derived dyes and lignin model compounds. Spectroscopic techniques, such as electron paramagnetic resonance and optical absorption spectroscopy, provide main tools to study how the enzymatic function is linked to the heme-pocket architecture, provided the experimental conditions are carefully chosen. Here, these techniques are used to investigate the effect of active site perturbations on the structure of ferric P-class DyP from

Indexed as

Water DecolorizationAmino AcidsBacterial ProteinsCatalytic DomainElectron Spin Resonance SpectroscopyGlycerolHemeHydrogen-Ion ConcentrationKlebsiella pneumoniaePeroxidaseAmino AcidsBacterial ProteinsGlycerolHemePeroxidaseactive site structurealkaline transitionelectron paramagnetic resonanceglassing agentsheme peroxidasesligand bindingUV-vis spectroscopy

Identifiers

PMID34576013

DOI10.3390/ijms22189849

PMCPMC8468270

OpenAlexW3201037013

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.