Evidence map›Paper›PMID 30559426›Full record

ArticleNature chemical biology2019

Metalloprotein switches that display chemical-dependent electron transfer in cells.

Joshua T Atkinson, Ian J Campbell, Emily E Thomas, Sheila C Bonitatibus, Sean J Elliott, George N Bennett, Jonathan J Silberg

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Tuning Extracellular Electron Transfer byACS synthetic biology · 2020
    Article
  18. The Journal of biological chemistry · 2020
    Article
  19. Article
  20. De novo design of symmetric ferredoxins that shuttle electrons in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Joshua T AtkinsonSystems, Synthetic, and Physical Biology Graduate Program, Rice University, Houston, TX, USA.ORCID http://orcid.org/0000-0001-9293-4123
Ian J CampbellBiochemistry and Cell Biology Graduate Program, Rice University, Houston, TX, USA.
Emily E ThomasBiochemistry and Cell Biology Graduate Program, Rice University, Houston, TX, USA.
Sheila C BonitatibusDepartment of Chemistry, Boston University, Boston, MA, USA.
Sean J ElliottDepartment of Chemistry, Boston University, Boston, MA, USA.ORCID http://orcid.org/0000-0003-0096-9551
George N BennettDepartment of BioSciences, Rice University, Houston, TX, USA.
Jonathan J SilbergDepartment of BioSciences, Rice University, Houston, TX, USA. joff@rice.edu.ORCID http://orcid.org/0000-0001-5612-0667
Rice University · USBoston University · US

Funding

HOUSTON AREA MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008280 · NIGMS · RICE UNIVERSITY · PI WENSEL, THEODORE G · 1988 to 2023
$8.0M
NIGMS NIH HHS T32 GM008280
6 · The paper itself

Abstract

Biological electron transfer is challenging to directly regulate using environmental conditions. To enable dynamic, protein-level control over energy flow in metabolic systems for synthetic biology and bioelectronics, we created ferredoxin logic gates that utilize transcriptional and post-translational inputs to control energy flow through a synthetic electron transfer pathway that is required for bacterial growth. These logic gates were created by subjecting a thermostable, plant-type ferredoxin to backbone fission and fusing the resulting fragments to a pair of proteins that self-associate, a pair of proteins whose association is stabilized by a small molecule, and to the termini of a ligand-binding domain. We show that the latter domain insertion design strategy yields an allosteric ferredoxin switch that acquires an oxygen-tolerant [2Fe-2S] cluster and can use different chemicals, including a therapeutic drug and an environmental pollutant, to control the production of a reduced metabolite in Escherichia coli and cell lysates.

Indexed as

Amino Acid SequenceElectronsElectron Spin Resonance SpectroscopyElectron TransportEscherichia coliFerredoxinsMetalloproteinsMutagenesis, Site-DirectedProtein Processing, Post-TranslationalFerredoxinsMetalloproteins

Identifiers

PMID30559426
PMCPMC6898983
OpenAlexW2903763445

What OpenQuestion holds

Textmetadata
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.