Evidence map›Paper›PMID 25732258›Full record

ArticleMolecular microbiology2015

Dimeric chlorite dismutase from the nitrogen-fixing cyanobacterium Cyanothece sp. PCC7425.

Irene Schaffner, Stefan Hofbauer, Michael Krutzler, Katharina F Pirker, Marzia Bellei, Gerhard Stadlmayr, Georg Mlynek, Kristina Djinovic-Carugo, Gianantonio Battistuzzi, Paul G Furtmüller and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  8. Review
  9. Structure and reactivity of chlorite dismutase nitrosyls.Journal of inorganic biochemistry · 2020
    Article
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  14. Review
  15. Article
  16. Active Sites of OBiochemistry · 2017
    Article
  17. Article
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  19. Independent evolution of four heme peroxidase superfamilies.Archives of biochemistry and biophysics · 2015
    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

12 authors at 4 institutions in 3 countries.

Irene SchaffnerDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria.
Stefan HofbauerDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria.
Michael KrutzlerDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria.
Katharina F PirkerDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria.
Marzia BelleiDepartment of Life Sciences, University of Modena and Reggio Emilia, 41125, Modena, Italy.
Gerhard StadlmayrDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria.
Georg MlynekDepartment for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
Kristina Djinovic-CarugoDepartment for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
Gianantonio BattistuzziDepartment of Chemistry and Geology, University of Modena and Reggio Emilia, 41125, Modena, Italy.
Paul G FurtmüllerDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria.
Holger DaimsDepartment of Microbiology and Ecosystem Science, Division of Microbial Ecology, University of Vienna, Vienna, Austria.
Christian ObingerDepartment of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190, Vienna, Austria.
BOKU University · ATMax Perutz Labs · ATUniversity of Modena and Reggio Emilia · ITUniversity of Vienna · AT

Funding

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

Abstract

It is demonstrated that cyanobacteria (both azotrophic and non-azotrophic) contain heme b oxidoreductases that can convert chlorite to chloride and molecular oxygen (incorrectly denominated chlorite 'dismutase', Cld). Beside the water-splitting manganese complex of photosystem II, this metalloenzyme is the second known enzyme that catalyses the formation of a covalent oxygen-oxygen bond. All cyanobacterial Clds have a truncated N-terminus and are dimeric (i.e. clade 2) proteins. As model protein, Cld from Cyanothece sp. PCC7425 (CCld) was recombinantly produced in Escherichia coli and shown to efficiently degrade chlorite with an activity optimum at pH 5.0 [kcat 1144 ± 23.8 s(-1), KM 162 ± 10.0 μM, catalytic efficiency (7.1 ± 0.6) × 10(6) M(-1) s(-1)]. The resting ferric high-spin axially symmetric heme enzyme has a standard reduction potential of the Fe(III)/Fe(II) couple of -126 ± 1.9 mV at pH 7.0. Cyanide mediates the formation of a low-spin complex with k(on)  = (1.6 ± 0.1) × 10(5) M(-1) s(-1) and k(off) = 1.4 ± 2.9 s(-1) (KD ∼ 8.6 μM). Both, thermal and chemical unfolding follows a non-two-state unfolding pathway with the first transition being related to the release of the prosthetic group. The obtained data are discussed with respect to known structure-function relationships of Clds. We ask for the physiological substrate and putative function of these O2 -producing proteins in (nitrogen-fixing) cyanobacteria.

Indexed as

BiocatalysisChloridesCyanidesCyanotheceEscherichia coliHemeKineticsModels, MolecularOxidoreductasesOxygenPhylogenyProtein MultimerizationRecombinant ProteinsChlorideschloritechlorite dismutaseCyanidesHemeOxidoreductasesOxygenRecombinant Proteins

Identifiers

PMID25732258
PMCPMC4973843
OpenAlexW1932875834

What OpenQuestion holds

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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.