Evidence map›Paper›PMID 20039132›Full record

ArticlePhotosynthesis research2010

Enzymatic properties of the ferredoxin-dependent nitrite reductase from Chlamydomonas reinhardtii. Evidence for hydroxylamine as a late intermediate in ammonia production.

Masakazu Hirasawa, Jatindra N Tripathy, Frederik Sommer, Ramasamy Somasundaram, Jung-Sung Chung, Matthew Nestander, Mahima Kruthiventi, Masoud Zabet-Moghaddam, Michael K Johnson, Sabeeha S Merchant and 2 more

Abstract read
In one paragraph

Article in Photosynthesis research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

13 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Redox Regulation of Salt Tolerance inInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Remembering David B. Knaff (1941-2016).Photosynthesis research · 2016
    Article
  9. Article
  10. Article
  11. Heme-bound nitroxyl, hydroxylamine, and ammonia ligands as intermediates in the reaction cycle of cytochrome c nitrite reductase: a theoretical study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014
    Article
  12. Article
  13. 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

12 authors at 4 institutions in 2 countries.

Masakazu HirasawaDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, 79409-1061, USA.
Jatindra N Tripathy
Frederik Sommer
Ramasamy Somasundaram
Jung-Sung Chung
Matthew Nestander
Mahima Kruthiventi
Masoud Zabet-Moghaddam
Michael K Johnson
Sabeeha S Merchant
James P Allen
David B Knaff
Texas Tech University · USUniversity of California, Los Angeles · USUniversity of Georgia · USArizona State University · US

Funding

Assembly of Biological Iron-Sulfur ClustersR01GM062524 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI JOHNSON, MICHAEL K. · 2001 to 2012
$2.7M
Assembly and Repair of Biological Iron-Sulfur ClustersR37GM062524 · NIGMS · UNIVERSITY OF GEORGIA · PI JOHNSON, MICHAEL K. · 2014 to 2018
$1.7M
NIGMS NIH HHS GM62524NIGMS NIH HHS R01 GM062524NIGMS NIH HHS R37 GM062524
6 · The paper itself

Abstract

The ferredoxin-dependent nitrite reductase from the green alga Chlamydomonas reinhardtii has been cloned, expressed in Escherichia coli as a His-tagged recombinant protein, and purified to homogeneity. The spectra, kinetic properties and substrate-binding parameters of the C. reinhardtii enzyme are quite similar to those of the ferredoxin-dependent spinach chloroplast nitrite reductase. Computer modeling, based on the published structure of spinach nitrite reductase, predicts that the structure of C. reinhardtii nitrite reductase will be similar to that of the spinach enzyme. Chemical modification studies and the ionic-strength dependence of the enzyme's ability to interact with ferredoxin are consistent with the involvement of arginine and lysine residues on C. reinhardtii nitrite reductase in electrostatically-stabilized binding to ferredoxin. The C. reinhardtii enzyme has been used to demonstrate that hydroxylamine can serve as an electron-accepting substrate for the enzyme and that the product of hydroxylamine reduction is ammonia, providing the first experimental evidence for the hypothesis that hydroxylamine, bound to the enzyme, can serve as a late intermediate during the reduction of nitrite to ammonia catalyzed by the enzyme.

Indexed as

AmmoniaBiocatalysisChlamydomonas reinhardtiiElectron Spin Resonance SpectroscopyFerredoxin-Nitrite ReductaseFerredoxinsHydroxylamineModels, MolecularNitritesOsmolar ConcentrationOxidation-ReductionProtein Structure, SecondaryRecombinant ProteinsSpinacia oleraceaAmmoniaFerredoxin-Nitrite ReductaseFerredoxinsHydroxylamineNitritesRecombinant Proteins

Identifiers

PMID20039132
PMCPMC2833264
OpenAlexW2112249689

What OpenQuestion holds

Textmetadata
LicenceTDM
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.