Evidence map›Paper›PMID 11283349›Full record

ArticleThe Plant cell2001

Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms.

N Frankenberg, K Mukougawa, T Kohchi, J C Lagarias

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

79 citing papers in PubMed, 237 citations in OpenAlex.

  1. Article
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  4. Article
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  7. Article
  8. Elucidating the origins of phycocyanobilin biosynthesis and phycobiliproteins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Protein-chromophore interactions controlling photoisomerization in red/green cyanobacteriochromes.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  10. Review
  11. Article
  12. Article
  13. Phytochromes inFrontiers in plant science · 2021
    Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Crystal structure of the first eukaryotic bilin reductaseThe Journal of biological chemistry · 2019
    Article
  19. Article
  20. Cloning ofGenes · 2019
    Article

19 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 2 countries.

N FrankenbergSection of Molecular and Cellular Biology, University of California at Davis, One Shields Avenue, Davis, California 95616, USA.
K Mukougawa
T Kohchi
J C Lagarias
Nara Institute of Science and Technology · JPUniversity of California, Davis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytobilins are linear tetrapyrrole precursors of the light-harvesting prosthetic groups of the phytochrome photoreceptors of plants and the phycobiliprotein photosynthetic antennae of cyanobacteria, red algae, and cryptomonads. Previous biochemical studies have established that phytobilins are synthesized from heme via the intermediacy of biliverdin IX alpha (BV), which is reduced subsequently by ferredoxin-dependent bilin reductases with different double-bond specificities. By exploiting the sequence of phytochromobilin synthase (HY2) of Arabidopsis, an enzyme that catalyzes the ferredoxin-dependent conversion of BV to the phytochrome chromophore precursor phytochromobilin, genes encoding putative bilin reductases were identified in the genomes of various cyanobacteria, oxyphotobacteria, and plants. Phylogenetic analyses resolved four classes of HY2-related genes, one of which encodes red chlorophyll catabolite reductases, which are bilin reductases involved in chlorophyll catabolism in plants. To test the catalytic activities of these putative enzymes, representative HY2-related genes from each class were amplified by the polymerase chain reaction and expressed in Escherichia coli. Using a coupled apophytochrome assembly assay and HPLC analysis, we examined the ability of the recombinant proteins to catalyze the ferredoxin-dependent reduction of BV to phytobilins. These investigations defined three new classes of bilin reductases with distinct substrate/product specificities that are involved in the biosynthesis of the phycobiliprotein chromophore precursors phycoerythrobilin and phycocyanobilin. Implications of these results are discussed with regard to the pathways of phytobilin biosynthesis and their evolution.

Indexed as

Amino Acid SequenceChromatography, High Pressure LiquidCyanobacteriaElectrophoresis, Polyacrylamide GelEscherichia coliEvolution, MolecularFerredoxinsMolecular Sequence DataOxidoreductasesPhylogenyPlantsPolymerase Chain ReactionRecombinant ProteinsSequence AlignmentSubstrate SpecificityFerredoxinsOxidoreductasesphytochromobilin synthaseRecombinant Proteins

Identifiers

PMID11283349
PMCPMC135530
OpenAlexW2160430130

What OpenQuestion holds

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Read underepoch 390

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.