Evidence map›Paper›PMID 31423350›Full record

ArticleACS catalysis2019

Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme

Lisa Milazzo, Thomas Gabler, Dominic Pühringer, Zuzana Jandova, Daniel Maresch, Hanna Michlits, Vera Pfanzagl, Kristina Djinović-Carugo, Chris Oostenbrink, Paul G Furtmüller and 3 more

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In one paragraph

Article in ACS catalysis, 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
1.3field-weighted citation impact, top 20% 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, 20 citations in OpenAlex.

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  11. Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.Computational and structural biotechnology journal · 2023
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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

13 authors at 4 institutions in 3 countries.

Lisa MilazzoDipartimento di Chimica "Ugo Schiff", Università di Firenze, Via della Lastruccia 3-13, I-50019 Sesto Fiorentino (FI), Italy.
Thomas GablerDepartment of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Dominic PühringerDepartment for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, A-1030 Vienna, Austria.
Zuzana JandovaDepartment of Material Sciences and Process Engineering, Institute of Molecular Modeling and Simulation, BOKU-University of Natural Resources and Life Sciences, A-1190 Vienna, Austria.
Daniel MareschDepartment of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Hanna MichlitsDepartment of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Vera PfanzaglDepartment of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Kristina Djinović-CarugoDepartment for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, A-1030 Vienna, Austria.
Chris OostenbrinkDepartment of Material Sciences and Process Engineering, Institute of Molecular Modeling and Simulation, BOKU-University of Natural Resources and Life Sciences, A-1190 Vienna, Austria.
Paul G FurtmüllerDepartment of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Christian ObingerDepartment of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Giulietta SmulevichDipartimento di Chimica "Ugo Schiff", Università di Firenze, Via della Lastruccia 3-13, I-50019 Sesto Fiorentino (FI), Italy.
Stefan HofbauerDepartment of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
BOKU University · ATUniversity of Florence · ITMax Perutz Labs · ATUniversity of Vienna · AT

Funding

Austrian Science Fund FWF P 29099Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Coproheme decarboxylase (ChdC) catalyzes the last step in the heme biosynthesis pathway of monoderm bacteria with coproheme acting both as redox cofactor and substrate. Hydrogen peroxide mediates the stepwise decarboxylation of propionates 2 and 4 of coproheme. Here we present the crystal structures of coproheme-loaded ChdC from

Identifiers

PMID31423350
PMCPMC6691569
OpenAlexW2951328527

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.