Evidence map›Paper›PMID 23027976›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Bacillus cereus iron uptake protein fishes out an unstable ferric citrate trimer.

Tatsuya Fukushima, Allyson K Sia, Benjamin E Allred, Rita Nichiporuk, Zhongrui Zhou, Ulla N Andersen, Kenneth N Raymond

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. The (Bio)Chemistry of Non-Transferrin-Bound Iron.Molecules (Basel, Switzerland) · 2022
    Review
  3. Article
  4. Hierarchical routing in carbon metabolism favors iron-scavenging strategy in iron-deficient soilProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Coordination Chemistry of Microbial Iron Transport.Accounts of chemical research · 2015
    Article
  11. Article
  12. Article
  13. Article
  14. Gram-positive siderophore-shuttle with iron-exchange from Fe-siderophore to apo-siderophore by Bacillus cereus YxeB.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

7 authors at 1 institution in 1 country.

Tatsuya FukushimaDepartment of Chemistry, University of California, Berkeley, CA 94720-1460, USA.
Allyson K Sia
Benjamin E Allred
Rita Nichiporuk
Zhongrui Zhou
Ulla N Andersen
Kenneth N Raymond
University of California, Berkeley · US

Funding

Coordination Chemistry of Microbial Iron Transport CompoundsR01AI011744 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI RAYMOND, KENNETH N · 1986 to 2013
$4.1M
QTOF MASS SPECTROMETER: CELL MOLECULAR BIOLOGY, PROTEIN STRUCTURES10RR022393 · NCRR · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2006 to 2006
$499k
NCRR NIH HHS 1S10RR022393-01NCRR NIH HHS S10 RR022393NIAID NIH HHS AI11744NIAID NIH HHS R01 AI011744
6 · The paper itself

Abstract

Citrate is a common biomolecule that chelates Fe(III). Many bacteria and plants use ferric citrate to fulfill their nutritional requirement for iron. Only the Escherichia coli ferric citrate outer-membrane transport protein FecA has been characterized; little is known about other ferric citrate-binding proteins. Here we report a unique siderophore-binding protein from the gram-positive pathogenic bacterium Bacillus cereus that binds multinuclear ferric citrate complexes. We have demonstrated that B. cereus ATCC 14579 takes up (55)Fe radiolabeled ferric citrate and that a protein, BC_3466 [renamed FctC (ferric citrate-binding protein C)], binds ferric citrate. The dissociation constant (K(d)) of FctC at pH 7.4 with ferric citrate (molar ratio 1:50) is 2.6 nM. This is the tightest binding observed of any B. cereus siderophore-binding protein. Nano electrospray ionization-mass spectrometry (nano ESI-MS) analysis of FctC and ferric citrate complexes or citrate alone show that FctC binds diferric di-citrate, and triferric tricitrate, but does not bind ferric di-citrate, ferric monocitrate, or citrate alone. Significantly, the protein selectively binds triferric tricitrate even though this species is naturally present at very low equilibrium concentrations.

Indexed as

Bacillus cereusBacterial ProteinsFerric CompoundsIron RadioisotopesIsotope LabelingMass SpectrometryMolecular StructureProtein BindingSiderophoresBacterial Proteinsferric citrateFerric CompoundsIron RadioisotopesSiderophores

Identifiers

PMID23027976
PMCPMC3479497
OpenAlexW2030012981

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.