Evidence map›Paper›PMID 27758026›Full record

ArticleThe FEBS journal2016

Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies.

Stefan Hofbauer, Georg Mlynek, Lisa Milazzo, Dominic Pühringer, Daniel Maresch, Irene Schaffner, Paul G Furtmüller, Giulietta Smulevich, Kristina Djinović-Carugo, Christian Obinger

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 44 citations in OpenAlex.

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  9. Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.Computational and structural biotechnology journal · 2023
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  19. Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020
    Review
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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

10 authors at 4 institutions in 3 countries.

Stefan HofbauerDepartment for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Austria.
Georg MlynekDepartment for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Austria.
Lisa MilazzoDipartimento di Chimica 'Ugo Schiff', Università di Firenze, Sesto Fiorentino (FI), Italy.
Dominic PühringerDepartment for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Austria.
Daniel MareschDivision of Biochemistry, Department of Chemistry, BOKU - University of Natural Resources and Life Sciences, Vienna, Austria.
Irene SchaffnerDivision of Biochemistry, Department of Chemistry, BOKU - University of Natural Resources and Life Sciences, Vienna, Austria.
Paul G FurtmüllerDivision of Biochemistry, Department of Chemistry, BOKU - University of Natural Resources and Life Sciences, Vienna, Austria.
Giulietta SmulevichDipartimento di Chimica 'Ugo Schiff', Università di Firenze, Sesto Fiorentino (FI), Italy.
Kristina Djinović-CarugoDepartment for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Austria.
Christian ObingerDivision of Biochemistry, Department of Chemistry, BOKU - University of Natural Resources and Life Sciences, Vienna, Austria.
BOKU University · ATMax Perutz Labs · ATUniversity of Florence · ITUniversity of Vienna · AT

Funding

Austrian Science Fund FWF I 2429Austrian Science Fund FWF P 25270Austrian Science Fund FWF P 29099Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Heme biosynthesis in Gram-positive bacteria follows a recently described coproporphyrin-dependent pathway with HemQ catalyzing the decarboxylation of coproheme to heme b. Here we present the first crystal structure of a HemQ (homopentameric coproheme-HemQ from Listeria monocytogenes) at 1.69 Å resolution and the conversion of coproheme to heme b followed by UV-vis and resonance Raman spectroscopy as well as mass spectrometry. The ferric five-coordinated coproheme iron of HemQ is weakly bound by a neutral proximal histidine H174. In the crystal structure of the resting state, the distal Q187 (conserved in Firmicutes HemQ) is H-bonded with propionate p2 and the hydrophobic distal cavity lacks solvent water molecules. Two H DATABASE: Structural data are available in the PDB under the accession number 5LOQ.

Indexed as

Amino Acid SequenceBacterial ProteinsCatalytic DomainCrystallography, X-RayGram-Positive BacteriaHemeHemeproteinsHeminHydrogen BondingHydrogen PeroxideKineticsListeria monocytogenesMass SpectrometryModels, MolecularPropionatesProtein BindingBacterial ProteinscoproheminHemeHemeproteinsHeminHydrogen PeroxidePropionatescoprohemeGram-positive pathogensheme bheme biosynthesisHemQ

Identifiers

PMID27758026
PMCPMC5157759
OpenAlexW2538555683

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.