Evidence map›Paper›PMID 30714018›Full record

ArticleChem2019

Charge Transfer between [4Fe4S] Proteins and DNA Is Unidirectional: Implications for Biomolecular Signaling.

Ruijie D Teo, Benjamin J G Rousseau, Elizabeth R Smithwick, Rosa Di Felice, David N Beratan, Agostino Migliore

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Chem, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. FeSBCP analogue from cyanobacteria: insights from in vitro and in silico studies.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2025
    Article
  3. Unveiling the charge transport blockade in the D2 branch of the photosystem II reaction center.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Multiple hops move electrons from bacteria to rocks.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Oxalate decarboxylase uses electron hole hopping for catalysis.The Journal of biological chemistry · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Mapping hole hopping escape routes in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Why Are DNA and Protein Electron Transfer So Different?Annual review of physical chemistry · 2019
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Ruijie D TeoDepartment of Chemistry, Duke University, Durham, NC 27708, United States.
Benjamin J G RousseauDepartment of Chemistry, Duke University, Durham, NC 27708, United States.
Elizabeth R SmithwickDepartment of Chemistry, Duke University, Durham, NC 27708, United States.
Rosa Di FeliceDepartment of Physics and Astronomy, University of Southern California, Los Angeles, CA 90089, United States.
David N BeratanDepartment of Chemistry, Duke University, Durham, NC 27708, United States.
Agostino MiglioreDepartment of Chemistry, Duke University, Durham, NC 27708, United States.
Duke University · USQB3 · US

Funding

MAPPING OF ELECTRON TUNNELING PATHWAYS IN PROTEINSR01GM048043 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI DAVID BERATAN · 1993 to 2026
$6.0M
NIGMS NIH HHS R01 GM048043
6 · The paper itself

Abstract

Recent experiments suggest that DNA-mediated charge transport might enable signaling between the [4Fe4S] clusters in the C-terminal domains of human DNA primase and polymerase α, as well as the signaling between other replication and repair high-potential [4Fe4S] proteins. Our theoretical study demonstrates that the redox signaling cannot be accomplished exclusively by DNA-mediated charge transport because part of the charge transfer chain has an unfavorable free energy profile. We show that hole or excess electron transfer between a [4Fe4S] cluster and a nucleic acid duplex through a protein medium can occur within microseconds in one direction, while it is kinetically hindered in the opposite direction. We present a set of signaling mechanisms that may occur with the assistance of oxidants or reductants, using the allowed charge transfer processes. These mechanisms would enable the coordinated action of [4Fe4S] proteins on DNA, engaging the [4Fe4S] oxidation state dependence of the protein-DNA binding affinity.

Identifiers

PMID30714018
PMCPMC6350243
OpenAlexW2898585504

What OpenQuestion holds

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LicenceTDM
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.