Evidence map›Paper›PMID 32234783›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase.

Chen-Song Dong, Wei-Lun Zhang, Qiao Wang, Yu-Shuai Li, Xiao Wang, Min Zhang, Lin Liu

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

15 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Exploring the structural landscape of universal stress proteins in Archaea.World journal of microbiology & biotechnology · 2025
    Review
  5. Article
  6. Transitioning enzyme catalysis towards photocatalysis.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Light dependent protochlorophyllide oxidoreductase: a succinct look.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. 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

7 authors at 1 institution in 1 country.

Chen-Song DongSchool of Life Sciences, Anhui University, 230601 Hefei, Anhui, China.
Wei-Lun ZhangSchool of Life Sciences, Anhui University, 230601 Hefei, Anhui, China.
Qiao WangSchool of Life Sciences, Anhui University, 230601 Hefei, Anhui, China.
Yu-Shuai LiSchool of Life Sciences, Anhui University, 230601 Hefei, Anhui, China.
Xiao WangSchool of Life Sciences, Anhui University, 230601 Hefei, Anhui, China.
Min ZhangSchool of Life Sciences, Anhui University, 230601 Hefei, Anhui, China.
Lin LiuSchool of Life Sciences, Anhui University, 230601 Hefei, Anhui, China; liulin@ahu.edu.cn.ORCID 0000-0002-9803-6540
Anhui University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) is the penultimate step of chlorophyll biosynthesis. In oxygenic photosynthetic bacteria, algae, and plants, this reaction can be catalyzed by the light-dependent Pchlide oxidoreductase (LPOR), a member of the short-chain dehydrogenase superfamily sharing a conserved Rossmann fold for NAD(P)H binding and the catalytic activity. Whereas modeling and simulation approaches have been used to study the catalytic mechanism of this light-driven reaction, key details of the LPOR structure remain unclear. We determined the crystal structures of LPOR from two cyanobacteria,

Indexed as

LightCatalysisChlorophyllCrystallography, X-RayCyanobacteriaModels, MolecularNADPOxidoreductases Acting on CH-CH Group DonorsProtein ConformationProtochlorophyllideProtonsSynechocystisThermosynechococcusChlorophyllNADPOxidoreductases Acting on CH-CH Group DonorsProtochlorophyllideprotochlorophyllide reductaseProtonschlorophyll biosynthesiscrystal structureNADPHphotocatalysisproton relay

Identifiers

PMID32234783
PMCPMC7165480
OpenAlexW3014166238

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.