Evidence map›Paper›PMID 28975508›Full record

ArticlePhotosynthesis research2017

Identification of the ferredoxin interaction sites on ferredoxin-dependent glutamate synthase from Synechocystis sp. PCC 6803.

Masakazu Hirasawa, Jacaranda Solis, Nanditha Vaidyanathan, Anurag P Srivastava, R Max Wynn, Roger B Sutton, David B Knaff

Abstract read
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In one paragraph

Article in Photosynthesis research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 48% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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 4 institutions in 1 country.

Masakazu HirasawaDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, 79409-1061, USA.
Jacaranda SolisCenter for Biotechnology and Genomics, Texas Tech University, Lubbock, TX, 79409-3132, USA.
Nanditha VaidyanathanCenter for Biotechnology and Genomics, Texas Tech University, Lubbock, TX, 79409-3132, USA.
Anurag P SrivastavaDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, 79409-1061, USA.
R Max WynnDepartments of Internal Medicine and Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, 75390-9038, USA. richard.wynn@utsouthwestern.edu.
Roger B SuttonDepartment of Cell Physiology and Molecular Biophysics, Texas Tech Health Science Center, Lubbock, TX, 79430-6551, USA.
David B KnaffDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, 79409-1061, USA.
Texas Tech University · USRosalind Franklin University of Medicine and Science · USTexas Tech University Health Sciences Center · USThe University of Texas Southwestern Medical Center · US

Funding

Human dysferlin and its implications in Limb-Girdle Muscular DystrophyR01AR063634 · NIAMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI SUTTON, ROGER BRYAN · 2014 to 2018
$1.8M
6 · The paper itself

Abstract

Based on in silico docking methods, five amino acids in glutamate synthase (Gln-467, His-1144, Asn-1147, Arg-1162, and Trp-676) likely constitute key binding residues in the interface of a glutamate synthase:ferredoxin complex. Although all interfacial mutants studied showed the ability to form a complex under low ionic strength, these docking mutations showed significantly less ferredoxin-dependent activities, while still retaining enzymatic activity. Furthermore, isothermal titration calorimetry showed a possible 1:2 molar ratio between the wild-type glutamate synthase and ferredoxin. However, each of our interfacial mutants showed only a 1:1 complex with ferredoxin, suggesting that the mutations directly affect the glutamate synthase:ferredoxin heterodimer interface.

Indexed as

Amino Acid OxidoreductasesCalorimetryCircular DichroismFerredoxinsHydrophobic and Hydrophilic InteractionsModels, MolecularStatic ElectricitySynechocystisThermodynamicsAmino Acid OxidoreductasesFerredoxinsglutamate synthase (ferredoxin)Electrostatic interactionsFerredoxinFlavin mononucleotide (FMN)Glutamate synthaseIn silico dockingIron–sulfur-binding sitesIsothermal titration calorimetrySite-directed mutagenesisSpectral perturbation

Identifiers

PMID28975508
OpenAlexW2763227671

What OpenQuestion holds

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Registered trials

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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.