Evidence map›Paper›PMID 24317397›Full record

ArticleJournal of bacteriology2014

Nonredundant roles for cytochrome c2 and two high-potential iron-sulfur proteins in the photoferrotroph Rhodopseudomonas palustris TIE-1.

Lina J Bird, Ivo H Saraiva, Shannon Park, Eduardo O Calçada, Carlos A Salgueiro, Wolfgang Nitschke, Ricardo O Louro, Dianne K Newman

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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Paramagnetic NMR to study iron sulfur proteins:Journal of biomolecular NMR · 2023
    Article
  6. Article
  7. Protein Interactions inMolecules (Basel, Switzerland) · 2023
    Article
  8. Article
  9. Frontiers in microbiology · 2022
    Review
  10. Article
  11. Biomolecular NMR assignments · 2020
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
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

8 authors at 4 institutions in 3 countries.

Lina J BirdDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Ivo H Saraiva
Shannon Park
Eduardo O Calçada
Carlos A Salgueiro
Wolfgang Nitschke
Ricardo O Louro
Dianne K Newman
Universidade Nova de Lisboa · PTCalifornia Institute of Technology · USCentre National de la Recherche Scientifique · FRHoward Hughes Medical Institute · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The purple bacterium Rhodopseudomonas palustris TIE-1 expresses multiple small high-potential redox proteins during photoautotrophic growth, including two high-potential iron-sulfur proteins (HiPIPs) (PioC and Rpal_4085) and a cytochrome c2. We evaluated the role of these proteins in TIE-1 through genetic, physiological, and biochemical analyses. Deleting the gene encoding cytochrome c2 resulted in a loss of photosynthetic ability by TIE-1, indicating that this protein cannot be replaced by either HiPIP in cyclic electron flow. PioC was previously implicated in photoferrotrophy, an unusual form of photosynthesis in which reducing power is provided through ferrous iron oxidation. Using cyclic voltammetry (CV), electron paramagnetic resonance (EPR) spectroscopy, and flash-induced spectrometry, we show that PioC has a midpoint potential of 450 mV, contains all the typical features of a HiPIP, and can reduce the reaction centers of membrane suspensions in a light-dependent manner at a much lower rate than cytochrome c2. These data support the hypothesis that PioC linearly transfers electrons from iron, while cytochrome c2 is required for cyclic electron flow. Rpal_4085, despite having spectroscopic characteristics and a reduction potential similar to those of PioC, is unable to reduce the reaction center. Rpal_4085 is upregulated by the divalent metals Fe(II), Ni(II), and Co(II), suggesting that it might play a role in sensing or oxidizing metals in the periplasm. Taken together, our results suggest that these three small electron transfer proteins perform different functions in the cell.

Indexed as

Bacterial ProteinsCytochromes c2Gene DeletionIron-Sulfur ProteinsLightMetalsOxidation-ReductionPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsRhodopseudomonasSpectrum AnalysisStatic ElectricityBacterial ProteinsCytochromes c2high potential iron-sulfur proteinIron-Sulfur ProteinsMetalsPhotosynthetic Reaction Center Complex Proteins

Identifiers

PMID24317397
PMCPMC3911180
OpenAlexW2144638420

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.