Evidence map›Paper›PMID 19586916›Full record

ArticleThe Journal of biological chemistry2009

Pattern of expression and substrate specificity of chloroplast ferredoxins from Chlamydomonas reinhardtii.

Aimee M Terauchi, Shu-Fen Lu, Mirko Zaffagnini, Shane Tappa, Masakazu Hirasawa, Jatindra N Tripathy, David B Knaff, Patrick J Farmer, Stéphane D Lemaire, Toshiharu Hase and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

64 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
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  8. Changing the tracks: screening for electron transfer proteins to support hydrogen production.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
  9. Review
  10. Article
  11. Diversification of Ferredoxins across Living Organisms.Current issues in molecular biology · 2021
    Article
  12. Review
  13. Article
  14. From economy to luxury: Copper homeostasis in Chlamydomonas and other algae.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  15. The Journal of biological chemistry · 2020
    Article
  16. Article
  17. Article
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  20. Article

4 more citing papers are in PubMed but not listed here.

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

11 authors at 7 institutions in 3 countries.

Aimee M TerauchiDepartment of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095-1569, USA.
Shu-Fen Lu
Mirko Zaffagnini
Shane Tappa
Masakazu Hirasawa
Jatindra N Tripathy
David B Knaff
Patrick J Farmer
Stéphane D Lemaire
Toshiharu Hase
Sabeeha S Merchant
Texas Tech University · USCentre National de la Recherche Scientifique · FRUCLA Health · USIrvine University · USProtein Research Foundation · JPUniversity of California, Irvine · USUniversity of California, Los Angeles · US

Funding

NIGMS NIH HHS GM070104
6 · The paper itself

Abstract

Ferredoxin (Fd) is the major iron-containing protein in photosynthetic organisms and is central to reductive metabolism in the chloroplast. The Chlamydomonas reinhardtii genome encodes six plant type [Fe2S2] ferredoxins, products of PETF, FDX2-FDX6. We performed the functional analysis of these ferredoxins by localizing Fd, Fdx2, Fdx3, and Fdx6 to the chloroplast by using isoform-specific antibodies and monitoring the pattern of gene expression by iron and copper nutrition, nitrogen source, and hydrogen peroxide stress. In addition, we also measured the midpoint redox potentials of Fd and Fdx2 and determined the kinetic parameters of their reactions with several ferredoxin-interacting proteins, namely nitrite reductase, Fd:NADP+ oxidoreductase, and Fd:thioredoxin reductase. We found that each of the FDX genes is differently regulated in response to changes in nutrient supply. Moreover, we show that Fdx2 (Em = -321 mV), whose expression is regulated by nitrate, is a more efficient electron donor to nitrite reductase relative to Fd. Overall, the results suggest that each ferredoxin isoform has substrate specificity and that the presence of multiple ferredoxin isoforms allows for the allocation of reducing power to specific metabolic pathways in the chloroplast under various growth conditions.

Indexed as

Algal ProteinsAnimalsBase SequenceChlamydomonas reinhardtiiChloroplastsCopperFerredoxinsGene Expression RegulationGenome, ChloroplastHydrogen PeroxideIronMolecular Sequence DataOxidantsOxidative StressOxidoreductasesProtozoan ProteinsAlgal ProteinsCopperFerredoxinsHydrogen PeroxideIronOxidantsOxidoreductasesProtozoan Proteins

Identifiers

PMID19586916
PMCPMC2757988
OpenAlexW2008216530

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.