Evidence map›Paper›PMID 33460502›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Electron Transfer from Haem to the Di-Iron Ferroxidase Centre in Bacterioferritin.

Jacob Pullin, Justin M Bradley, Geoffrey R Moore, Nick E Le Brun, Michael T Wilson, Dimitri A Svistunenko

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. The assembly rules guiding hetero-oligomeric bacterioferritin organization and their evolutionary signature.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Biomolecules · 2022
    Article
  10. Iron Oxidation inAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  11. Article
  12. Electron Transfer from Haem to the Di-Iron Ferroxidase Centre in Bacterioferritin.Angewandte Chemie (International ed. in English) · 2021
    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

6 authors at 2 institutions in 1 country.

Jacob PullinSchool of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, UK.ORCID 0000-0002-8186-8543
Justin M BradleySchool of Chemistry, University of East Anglia, Norwich Research Park, Norwich, Norfolk, NR4 7TJ, UK.ORCID 0000-0003-1635-4455
Geoffrey R MooreSchool of Chemistry, University of East Anglia, Norwich Research Park, Norwich, Norfolk, NR4 7TJ, UK.
Nick E Le BrunSchool of Chemistry, University of East Anglia, Norwich Research Park, Norwich, Norfolk, NR4 7TJ, UK.
Michael T WilsonSchool of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, UK.
Dimitri A SvistunenkoSchool of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, UK.ORCID 0000-0001-8060-2738
University of East Anglia · GBUniversity of Essex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R002363/1Biotechnology and Biological Sciences Research Council BB/R003203/1
6 · The paper itself

Abstract

The iron redox cycle in ferritins is not completely understood. Bacterioferritins are distinct from other ferritins in that they contain haem groups. It is acknowledged that the two iron motifs in bacterioferritins, the di-nuclear ferroxidase centre and the haem B group, play key roles in two opposing processes, iron sequestration and iron mobilisation, respectively, and the two redox processes are independent. Herein, we show that in Escherichia coli bacterioferritin, there is an electron transfer pathway from the haem to the ferroxidase centre suggesting a new role(s) haem might play in bacterioferritins.

Indexed as

Bacterial ProteinsCeruloplasminCytochrome b GroupElectron TransportEscherichia coliFerritinsHemeBacterial ProteinsbacterioferritinCeruloplasminCytochrome b GroupFerritinsHemeelectron transferferritinsferroxidase centremetalloproteinsstopped-flow spectrophotometry

Identifiers

PMID33460502
PMCPMC8048850
OpenAlexW3121551002

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.