Evidence map›Paper›PMID 21505944›Full record

ArticlePhotosynthesis research2011

The relationship between different spectral forms of the protochlorophyllide oxidoreductase complex and the structural organisation of prolamellar bodies isolated from Zea mays.

Eva Selstam, Anthony P R Brain, W Patrick Williams

Abstract read
PubMed Publisher
In one paragraph

Article in Photosynthesis research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Spatial Nano-Morphology of the Prolamellar Body in EtiolatedFrontiers in cell and developmental biology · 2020
    Article
  3. 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

3 authors.

Eva SelstamUmeå Plant Science Centre, Department of Plant Physiology, University of Umeå, Umeå, Sweden. eva.selstam@plantphys.umu.se
Anthony P R Brain
W Patrick Williams

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Incubation of prolamellar bodies (PLB) in high-salt media leads to changes in PLB structure and properties of their protochlorophyllide oxidoreductase-protochlorophyllide (POR-PChlide) complex. The paracrystalline organisation typical of PLB is disrupted and NADPH dissociates from photoconvertible POR-PChlide, with absorption maxima at 640 and 650 nm (POR-PChlide (640/650)), and a non-photoconvertible form, with absorption maxima at 635 nm (POR-PChlide (635)), is formed. These effects are strongly dependent on the valence of the cation of the perturbing salt, indicating that they involve surface double layers effects. They are also influenced by the nature of the anion and by high concentrations of non-electrolytes, suggesting the involvement of surface hydration effects. The structural changes are largely, if not entirely, independent of the presence of excess NADPH. Changes to the POR-PChlide complex, however, are strongly inhibited by excess NADPH suggesting that the two sets of changes may not be causally linked. As long as the disruption is not too great, the structural changes seen on incubation of PLB in high salt media lacking excess NADPH are reversed on removal of the high salt perturbation. This reversal is independent of the presence or absence of added NADPH. Reformation of photoconvertible POR-PChlide, however, requires the presence of NADPH. The reformation of paracrystalline PLB in the absence of NADPH strongly indicates that preservation of PLB structure, in isolated PLB preparations at least, is independent of the presence or absence of POR-PChlide (650).

Indexed as

AnionsCationsChlorophyllElectrolytesMicroscopy, Electron, TransmissionNADPOrganellesOxidoreductases Acting on CH-CH Group DonorsProtein IsoformsSaltsSeedlingsSpectrometry, FluorescenceZea maysAnionsCationsChlorophyllElectrolytesNADPOxidoreductases Acting on CH-CH Group DonorsProtein Isoformsprotochlorophyllide reductaseSalts

Identifiers

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.