Evidence map›Paper›PMID 24794567›Full record

ArticleJournal of bacteriology2014

The terminal oxidase cbb3 functions in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense.

Yingjie Li, Oliver Raschdorf, Karen T Silva, Dirk Schüler

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. 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
1.4field-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

19 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. MagnetotacticISME communications · 2026
    Article
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  12. Review
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  15. Article
  16. Magnetosome biogenesis in magnetotactic bacteria.Nature reviews. Microbiology · 2016
    Review
  17. Article
  18. Article
  19. 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

4 authors at 3 institutions in 1 country.

Yingjie LiLudwig Maximilians Universität München, Department Biologie I, Mikrobiologie, Planegg-Martinsried, Germany.
Oliver RaschdorfLudwig Maximilians Universität München, Department Biologie I, Mikrobiologie, Planegg-Martinsried, Germany Max Planck Institute of Biochemistry, Department of Molecular Structural Biology, Martinsried, Germany.
Karen T SilvaLudwig Maximilians Universität München, Department Biologie I, Mikrobiologie, Planegg-Martinsried, Germany.
Dirk SchülerUniversität Bayreuth, Lehrstuhl f. Mikrobiologie, Bayreuth, Germany dirk.schueler@lrz.uni-muenchen.de.
Ludwig-Maximilians-Universität München · DEMax Planck Institute of Biochemistry · DEUniversity of Bayreuth · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biomineralization of magnetosomes in Magnetospirillum gryphiswaldense and other magnetotactic bacteria occurs only under suboxic conditions. However, the mechanism of oxygen regulation and redox control of biosynthesis of the mixed-valence iron oxide magnetite [FeII(FeIII)2O4] is still unclear. Here, we set out to investigate the role of aerobic respiration in both energy metabolism and magnetite biomineralization of M. gryphiswaldense. Although three operons encoding putative terminal cbb3-type, aa3-type, and bd-type oxidases were identified in the genome assembly of M. gryphiswaldense, genetic and biochemical analyses revealed that only cbb3 and bd are required for oxygen respiration, whereas aa3 had no physiological significance under the tested conditions. While the loss of bd had no effects on growth and magnetosome synthesis, inactivation of cbb3 caused pleiotropic effects under microaerobic conditions in the presence of nitrate. In addition to their incapability of simultaneous nitrate and oxygen reduction, cbb3-deficient cells had complex magnetosome phenotypes and aberrant morphologies, probably by disturbing the redox balance required for proper growth and magnetite biomineralization. Altogether, besides being the primary terminal oxidase for aerobic respiration, cbb3 oxidase may serve as an oxygen sensor and have a further role in poising proper redox conditions required for magnetite biomineralization.

Indexed as

Electron Transport Complex IVFerrosoferric OxideGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicGenome, BacterialMagnetospirillumOxidation-Reductioncbb3 oxidaseElectron Transport Complex IVFerrosoferric Oxide

Identifiers

PMID24794567
PMCPMC4097590
OpenAlexW1988511972

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.