Evidence map›Paper›PMID 36706455›Full record

ArticleBiochemistry2023

Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine.

Daniel Schmidt, Nikolaus Falb, Ilenia Serra, Marzia Bellei, Vera Pfanzagl, Stefan Hofbauer, Sabine Van Doorslaer, Gianantonio Battistuzzi, Paul G Furtmüller, Christian Obinger

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

10 authors at 3 institutions in 3 countries.

Daniel SchmidtInstitute of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, A-1190Vienna, Austria.ORCID 0000-0002-0655-654X
Nikolaus FalbInstitute of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, A-1190Vienna, Austria.
Ilenia SerraBIMEF Laboratory, Department of Chemistry, University of Antwerp, 2000Antwerp, Belgium.ORCID 0000-0003-4537-9635
Marzia BelleiDepartment of Life Sciences, University of Modena and Reggio Emilia, 41100Modena, Italy.
Vera PfanzaglInstitute of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, A-1190Vienna, Austria.ORCID 0000-0002-9361-8365
Stefan HofbauerInstitute of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, A-1190Vienna, Austria.ORCID 0000-0003-3375-7715
Sabine Van DoorslaerBIMEF Laboratory, Department of Chemistry, University of Antwerp, 2000Antwerp, Belgium.ORCID 0000-0002-1685-9202
Gianantonio BattistuzziDepartment of Chemistry and Geology, University of Modena and Reggio Emilia, 41100Modena, Italy.ORCID 0000-0003-4716-5745
Paul G FurtmüllerInstitute of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, A-1190Vienna, Austria.ORCID 0000-0002-1199-2469
Christian ObingerInstitute of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, A-1190Vienna, Austria.ORCID 0000-0002-7133-3430
BOKU University · ATUniversity of Antwerp · BEUniversity of Modena and Reggio Emilia · IT

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

The heme enzyme chlorite dismutase (Cld) catalyzes the degradation of chlorite to chloride and dioxygen. Many questions about the molecular reaction mechanism of this iron protein have remained unanswered, including the electronic nature of the catalytically relevant oxoiron(IV) intermediate and its interaction with the distal, flexible, and catalytically active arginine. Here, we have investigated the dimeric Cld from

Indexed as

ArginineSerotoninChloridesHydrogen-Ion ConcentrationKineticsOxidoreductasesArginineChlorideschloritechlorite dismutaseOxidoreductasesSerotonin

Identifiers

PMID36706455
PMCPMC9910045
OpenAlexW4318261414

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.