Evidence map›Paper›PMID 25826316›Full record

ArticlePloS one2015

Molecular insights into frataxin-mediated iron supply for heme biosynthesis in Bacillus subtilis.

Andreas Mielcarek, Bastian Blauenburg, Marcus Miethke, Mohamed A Marahiel

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Metabolic engineering ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Review
  3. Article
  4. Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.Computational and structural biotechnology journal · 2023
    Review
  5. InFrontiers in genetics · 2023
    Article
  6. Article
  7. Making and breaking heme.Current opinion in structural biology · 2019
    Review
  8. Article
  9. Article
  10. [Drug resistance and protoporphyrin ferrochelatase ofZhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2017
    Article
  11. Metal homeostasis and resistance in bacteria.Nature reviews. Microbiology · 2017
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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 2 institutions in 2 countries.

Andreas MielcarekPhilipps-University Marburg, Department of Chemistry/Biochemistry, Marburg, Germany.
Bastian BlauenburgPhilipps-University Marburg, Department of Chemistry/Biochemistry, Marburg, Germany.
Marcus MiethkePhilipps-University Marburg, Department of Chemistry/Biochemistry, Marburg, Germany; Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, California, United States of America.
Mohamed A MarahielPhilipps-University Marburg, Department of Chemistry/Biochemistry, Marburg, Germany.
Philipps University of Marburg · DEUniversity of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Iron is required as an element to sustain life in all eukaryotes and most bacteria. Although several bacterial iron acquisition strategies have been well explored, little is known about the intracellular trafficking pathways of iron and its entry into the systems for co-factor biogenesis. In this study, we investigated the iron-dependent process of heme maturation in Bacillus subtilis and present, for the first time, structural evidence for the physical interaction of a frataxin homologue (Fra), which is suggested to act as a regulatory component as well as an iron chaperone in different cellular pathways, and a ferrochelatase (HemH), which catalyses the final step of heme b biogenesis. Specific interaction between Fra and HemH was observed upon co-purification from crude cell lysates and, further, by using the recombinant proteins for analytical size-exclusion chromatography. Hydrogen-deuterium exchange experiments identified the landscape of the Fra/HemH interaction interface and revealed Fra as a specific ferrous iron donor for the ferrochelatase HemH. The functional utilisation of the in vitro-generated heme b co-factor upon Fra-mediated iron transfer was confirmed by using the B. subtilis nitric oxide synthase bsNos as a metabolic target enzyme. Complementary mutational analyses confirmed that Fra acts as an essential component for maturation and subsequent targeting of the heme b co-factor, hence representing a key player in the iron-dependent physiology of B. subtilis.

Indexed as

Bacillus subtilisFrataxinHemeIronIron-Binding ProteinsFrataxinHemeIronIron-Binding Proteins

Identifiers

PMID25826316
PMCPMC4380498
OpenAlexW2132852127

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.