Evidence map›Paper›PMID 37071675›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Elucidating the origins of phycocyanobilin biosynthesis and phycobiliproteins.

Nathan C Rockwell, Shelley S Martin, J Clark Lagarias

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.2field-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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Genome Assembly and Annotation for the Okinawan Green Marine Spoon WormInternational journal of molecular sciences · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Key Nutrient Drivers for Biomass and C-Phycocyanin Production inInternational journal of molecular sciences · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Cyanobacteriochromes: A Rainbow of Photoreceptors.Annual review of microbiology · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. Elucidating the origins of phycocyanobilin biosynthesis and phycobiliproteins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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 at 1 institution in 1 country.

Nathan C RockwellCollege of Biological Sciences, Department of Molecular and Cell Biology, University of California at Davis, Davis, CA 95616.ORCID 0000-0002-7748-7019
Shelley S MartinCollege of Biological Sciences, Department of Molecular and Cell Biology, University of California at Davis, Davis, CA 95616.
J Clark LagariasCollege of Biological Sciences, Department of Molecular and Cell Biology, University of California at Davis, Davis, CA 95616.ORCID 0000-0002-2093-0403
University of California, Davis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Terrestrial ecosystems and human societies depend on oxygenic photosynthesis, which began to reshape our atmosphere approximately 2.5 billion years ago. The earliest known organisms carrying out oxygenic photosynthesis are the cyanobacteria, which use large complexes of phycobiliproteins as light-harvesting antennae. Phycobiliproteins rely on phycocyanobilin (PCB), a linear tetrapyrrole (bilin) chromophore, as the light-harvesting pigment that transfers absorbed light energy from phycobilisomes to the chlorophyll-based photosynthetic apparatus. Cyanobacteria synthesize PCB from heme in two steps: A heme oxygenase converts heme into biliverdin IXα (BV), and the ferredoxin-dependent bilin reductase (FDBR) PcyA then converts BV into PCB. In the current work, we examine the origins of this pathway. We demonstrate that PcyA evolved from pre-PcyA proteins found in nonphotosynthetic bacteria and that pre-PcyA enzymes are active FDBRs that do not yield PCB. Pre-PcyA genes are associated with two gene clusters. Both clusters encode bilin-binding globin proteins, phycobiliprotein paralogs that we designate as BBAGs (bilin biosynthesis-associated globins). Some cyanobacteria also contain one such gene cluster, including a BBAG, two V4R proteins, and an iron-sulfur protein. Phylogenetic analysis shows that this cluster is descended from those associated with pre-PcyA proteins and that light-harvesting phycobiliproteins are also descended from BBAGs found in other bacteria. We propose that PcyA and phycobiliproteins originated in heterotrophic, nonphotosynthetic bacteria and were subsequently acquired by cyanobacteria.

Indexed as

CyanobacteriaPhycobiliproteinsBile PigmentsEcosystemHumansOxidoreductasesPhycobilinsPhycocyaninPhylogenyBile PigmentsOxidoreductasesPhycobilinsPhycobiliproteinsPhycocyaninphycocyanobilincyanobacteriochromelight harvesting antennaephycobilisomephylogenetic analysisphytochrome

Identifiers

PMID37071675
PMCPMC10151467
OpenAlexW4366235015

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.