Evidence map›Paper›PMID 18413861›Full record

ArticleProtein science : a publication of the Protein Society2008

Hydrodynamic characterization of the SufBC and SufCD complexes and their interaction with fluorescent adenosine nucleotides.

Arsen Petrovic, Colin T Davis, Kaveri Rangachari, Barbara Clough, R J M Iain Wilson, John F Eccleston

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2008. 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
2.1field-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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. SmsB-SmsC machinery inApplied and environmental microbiology · 2025
    Article
  3. Review
  4. Article
  5. Fe-S cluster biogenesis by the bacterial Suf pathway.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  6. Iron-sulfur clusters biogenesis by the SUF machinery: close to the molecular mechanism understanding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Building Fe-S proteins: bacterial strategies.Nature reviews. Microbiology · 2010
    Review
  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

6 authors at 1 institution in 1 country.

Arsen PetrovicMRC National Institute for Medical Research, London NW7 1AA, United Kingdom.
Colin T Davis
Kaveri Rangachari
Barbara Clough
R J M Iain Wilson
John F Eccleston
LifeArc · GB

Funding

Medical Research Council MC_U117532072
6 · The paper itself

Abstract

Bacteria, as well as the plastid organelles of algae and higher plants, utilize proteins of the suf operon. These are involved in Fe-S cluster assembly, particularly under conditions of iron limitation or oxidative stress. Genetic experiments in some organisms found that the ATPase SufC is essential, though its role in Fe-S biogenesis remains unclear. To ascertain how interactions with other individual Suf proteins affect the activity of SufC we coexpressed it with either SufB or SufD from Thermotoga maritima and purified the resulting SufBC and SufCD complexes. Analytical ultracentrifuge and multiangle light-scattering measurements showed that the SufBC complex exists in solution as the tetrameric SufB(2)C(2) species, whereas SufCD exists as an equilibrium mixture of SufCD and SufC(2)D(2). Transient kinetic studies of the complexes were made using fluorescent 2'(3')-O-(N-methylanthraniloyl-(mant) analogues of ATP and ADP. Both SufBC and SufCD bound mantATP and mantADP much more tightly than does SufC alone. Compared to the cleavage step of the mantATPase of SufC alone, that of SufBC was accelerated 180-fold and that of SufCD only fivefold. Given that SufB and SufD have 20% sequence identity and similar predicted secondary structures, the different hydrodynamic properties and kinetic mechanisms of the two complexes are discussed.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateBacterial ProteinsElectrophoresis, Polyacrylamide GelFluorescent DyesKineticsSpectrometry, FluorescenceAdenosine DiphosphateAdenosine TriphosphateBacterial ProteinsFluorescent Dyes

Identifiers

PMID18413861
PMCPMC2441996
OpenAlexW1984943283

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.