Evidence map›Paper›PMID 10449801›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Protochlorophyllide oxidoreductase B-catalyzed protochlorophyllide photoreduction in vitro: insight into the mechanism of chlorophyll formation in light-adapted plants.

N Lebedev, M P Timko

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Light dependent protochlorophyllide oxidoreductase: a succinct look.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Review
  3. Enzymes degraded under high light maintain proteostasis by transcriptional regulation inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Photoprotective role of NADPH:protochlorophyllide oxidoreductase A.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Enzymology below 200 K: the kinetics and thermodynamics of the photochemistry catalyzed by protochlorophyllide oxidoreductase.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  17. Article
  18. Article
  19. Article
  20. The protochlorophyllide-chlorophyllide cycle.Photosynthesis research · 2001
    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

2 authors at 1 institution in 1 country.

N LebedevDepartment of Biology, University of Virginia, Charlottesville, VA 22903, USA.
M P Timko
University of Virginia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism of the protochlorophyllide (PChlide) photoreduction reaction operating in light-adapted plants and catalyzed by NADPH:protochlorophyllide oxidoreductase B (PORb) has been analyzed by low-temperature fluorescence spectroscopy by using purified barley PORb overexpressed heterologously in Escherichia coli as a fusion protein with the maltose-binding protein. We show that the PORb-catalyzed PChlide reduction reaction consists of two steps, one photochemical and the other nonphotochemical. The initial photochemical reaction follows a single quantum mechanism and leads to the formation of an unstable intermediate with mixed pigment electronic structure and an EPR spectrum that suggests the presence of a free electron. The second step involves the spontaneous conversion of the unstable intermediate into chlorophyllide as defined by its spectroscopic characteristics and migration on an HPLC column. Both steps of the reaction can be performed at subzero temperatures in frozen samples, suggesting that they do not include major changes in enzyme conformation or pigment rearrangement within the active site. The rate of the reaction at room temperature depends linearly on enzyme and substrate (PChlide) concentration, and the kinetic parameters are consistent with one molecule of substrate bound per active monomer in solution. The PORb-catalyzed reaction in vitro is spectroscopically similar to that identified in leaves of light-adapted plants, suggesting that the same reaction sequence observed operates in planta.

Indexed as

ATP-Binding Cassette TransportersEscherichia coli ProteinsMonosaccharide Transport ProteinsOxidoreductases Acting on CH-CH Group DonorsAdaptation, PhysiologicalCarrier ProteinsCatalysisChlorophyllElectrophoresis, Polyacrylamide GelLightMaltose-Binding ProteinsOxidation-ReductionOxidoreductasesPlantsProtochlorophyllideRecombinant Fusion ProteinsATP-Binding Cassette TransportersCarrier ProteinsChlorophyllEscherichia coli ProteinsMaltose-Binding Proteinsmaltose transport system, E coliMonosaccharide Transport ProteinsOxidoreductasesOxidoreductases Acting on CH-CH Group DonorsProtochlorophyllideprotochlorophyllide reductaseRecombinant Fusion Proteins

Identifiers

PMID10449801
PMCPMC22317
OpenAlexW2057286743

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.