Evidence map›Paper›PMID 28334877›Full record

ArticleNucleic acids research2017

Iron mediates catalysis of nucleic acid processing enzymes: support for Fe(II) as a cofactor before the great oxidation event.

C Denise Okafor, Kathryn A Lanier, Anton S Petrov, Shreyas S Athavale, Jessica C Bowman, Nicholas V Hud, Loren Dean Williams

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Iron: Life's primeval transition metal.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Review
  8. Discovering riboswitches: the past and the future.Trends in biochemical sciences · 2023
    Review
  9. Reconsidering theACS bio & med chem Au · 2022
    Article
  10. Iron-responsive riboswitches.Current opinion in chemical biology · 2022
    Review
  11. Article
  12. Metals Are Integral to Life as We Know It.Frontiers in cell and developmental biology · 2022
    Article
  13. Article
  14. Article
  15. 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
  16. Multiple prebiotic metals mediate translation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Article
  18. In the Beginning was a Mutualism - On the Origin of Translation.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2018
    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

7 authors at 1 institution in 1 country.

C Denise OkaforSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332 0400, USA.
Kathryn A LanierSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332 0400, USA.
Anton S PetrovSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332 0400, USA.
Shreyas S AthavaleSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332 0400, USA.
Jessica C BowmanSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332 0400, USA.
Nicholas V HudSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332 0400, USA.
Loren Dean WilliamsSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332 0400, USA.
Georgia Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Life originated in an anoxic, Fe2+-rich environment. We hypothesize that on early Earth, Fe2+ was a ubiquitous cofactor for nucleic acids, with roles in RNA folding and catalysis as well as in processing of nucleic acids by protein enzymes. In this model, Mg2+ replaced Fe2+ as the primary cofactor for nucleic acids in parallel with known metal substitutions of metalloproteins, driven by the Great Oxidation Event. To test predictions of this model, we assay the ability of nucleic acid processing enzymes, including a DNA polymerase, an RNA polymerase and a DNA ligase, to use Fe2+ in place of Mg2+ as a cofactor during catalysis. Results show that Fe2+ can indeed substitute for Mg2+ in catalytic function of these enzymes. Additionally, we use calculations to unravel differences in energetics, structures and reactivities of relevant Mg2+ and Fe2+ complexes. Computation explains why Fe2+ can be a more potent cofactor than Mg2+ in a variety of folding and catalytic functions. We propose that the rise of O2 on Earth drove a Fe2+ to Mg2+ substitution in proteins and nucleic acids, a hypothesis consistent with a general model in which some modern biochemical systems retain latent abilities to revert to primordial Fe2+-based states when exposed to pre-GOE conditions.

Indexed as

CatalysisCoenzymesDNA-Directed DNA PolymeraseDNA-Directed RNA PolymerasesDNA LigasesIronMagnesiumOxidation-ReductionViral Proteinsbacteriophage T7 RNA polymeraseCoenzymesDeep Vent DNA polymeraseDNA-Directed DNA PolymeraseDNA-Directed RNA PolymerasesDNA LigasesIronMagnesiumViral Proteins

Identifiers

PMID28334877
PMCPMC5397171
OpenAlexW2607024535

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.