Evidence map›Paper›PMID 24778258›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Evolutionary history of redox metal-binding domains across the tree of life.

Arye Harel, Yana Bromberg, Paul G Falkowski, Debashish Bhattacharya

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. On the emergence of metabolism: the evolution of proteins that powered life.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  3. Article
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  12. Emergence of metal selectivity and promiscuity in metalloenzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Review
  13. Review
  14. Article
  15. Acetyl Phosphate as a Primordial Energy Currency at the Origin of Life.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2018
    Article
  16. Modular origins of biological electron transfer chains.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Review
  18. Article
  19. Article
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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.

Arye HarelEnvironmental Biophysics and Molecular Ecology Program, Institute of Marine and Coastal Science.
Yana BrombergDepartment of Biochemistry and Microbiology, and.
Paul G FalkowskiEnvironmental Biophysics and Molecular Ecology Program, Institute of Marine and Coastal Science,Department of Earth and Planetary Sciences, Rutgers University, The State University of New Jersey, Piscataway, NJ 08854 falko@marine.rutgers.edu.
Debashish BhattacharyaDepartment of Ecology, Evolution, and Natural Resources, Rutgers, The State University of New Jersey, New Brunswick, NJ 08901; and.
Rutgers, The State University of New Jersey · USInstitute of Marine and Coastal Research · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidoreductases mediate electron transfer (i.e., redox) reactions across the tree of life and ultimately facilitate the biologically driven fluxes of hydrogen, carbon, nitrogen, oxygen, and sulfur on Earth. The core enzymes responsible for these reactions are ancient, often small in size, and highly diverse in amino acid sequence, and many require specific transition metals in their active sites. Here we reconstruct the evolution of metal-binding domains in extant oxidoreductases using a flexible network approach and permissive profile alignments based on available microbial genome data. Our results suggest there were at least 10 independent origins of redox domain families. However, we also identified multiple ancient connections between Fe2S2- (adrenodoxin-like) and heme- (cytochrome c) binding domains. Our results suggest that these two iron-containing redox families had a single common ancestor that underwent duplication and divergence. The iron-containing protein family constitutes ∼50% of all metal-containing oxidoreductases and potentially catalyzed redox reactions in the Archean oceans. Heme-binding domains seem to be derived via modular evolutionary processes that ultimately form the backbone of redox reactions in both anaerobic and aerobic respiration and photosynthesis. The empirically discovered network allows us to peer into the ancient history of microbial metabolism on our planet.

Indexed as

Evolution, MolecularAdrenodoxinAmino Acid SequenceArchaeaBacteria, AnaerobicCytochromes cEcosystemEnergy MetabolismFerrous CompoundsHemeIronMolecular Sequence DataOxidation-ReductionOxidoreductasesOxygenProkaryotic CellsAdrenodoxinCytochromes cFerrous Compoundsferrous sulfateHemeIronOxidoreductasesOxygenbiogeochemical cyclescore pathwaysGreat Oxidation/Oxygenation Eventiron–sulfur

Identifiers

PMID24778258
PMCPMC4024910
OpenAlexW2108893642

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.