Evidence map›Paper›PMID 35994638›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Control of protein activity by photoinduced spin polarized charge reorganization.

Shirsendu Ghosh, Koyel Banerjee-Ghosh, Dorit Levy, David Scheerer, Inbal Riven, Jieun Shin, Harry B Gray, Ron Naaman, Gilad Haran

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Chiral Induced Spin Selectivity.Chemical reviews · 2024
    Review
  7. New Perspective on Electron Transfer through Molecules.The journal of physical chemistry letters · 2022
    Article
  8. 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

9 authors at 2 institutions in 3 countries.

Shirsendu GhoshDepartment of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0002-0820-9349
Koyel Banerjee-GhoshDepartment of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0002-1376-5198
Dorit LevyDepartment of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.
David ScheererDepartment of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0002-6641-6629
Inbal RivenDepartment of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.
Jieun ShinBeckman Institute, California Institute of Technology, Pasadena, CA 91125.
Harry B GrayBeckman Institute, California Institute of Technology, Pasadena, CA 91125.ORCID 0000-0002-7937-7876
Ron NaamanDepartment of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0003-1910-366X
Gilad HaranDepartment of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0003-1837-9779
Weizmann Institute of Science · ILCalifornia Institute of Technology · US

Funding

ELECTRON-TRANSFER PROCESSES IN IRON AND COPPER PROTEINSR01DK019038 · NIDDK · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI GRAY, HARRY B, WINKLER, JAY R · 1986 to 2023
$7.0M
NIDDK NIH HHS R01 DK019038
6 · The paper itself

Abstract

Considerable electric fields are present within living cells, and the role of bioelectricity has been well established at the organismal level. Yet much remains to be learned about electric-field effects on protein function. Here, we use phototriggered charge injection from a site-specifically attached ruthenium photosensitizer to directly demonstrate the effect of dynamic charge redistribution within a protein. We find that binding of an antibody to phosphoglycerate kinase (PGK) is increased twofold under illumination. Remarkably, illumination is found to suppress the enzymatic activity of PGK by a factor as large as three. These responses are sensitive to the photosensitizer position on the protein. Surprisingly, left (but not right) circularly polarized light elicits these responses, indicating that the electrons involved in the observed dynamics are spin polarized, due to spin filtration by protein chiral structures. Our results directly establish the contribution of electrical polarization as an allosteric signal within proteins. Future experiments with phototriggered charge injection will allow delineation of charge rearrangement pathways within proteins and will further depict their effects on protein function.

Indexed as

Electromagnetic FieldsProteinsAllosteric RegulationElectronsLightingPhotosensitizing AgentsProtein BindingRutheniumPhotosensitizing AgentsProteinsRutheniumallosterychiral-induced spin selectivityenzymatic activitypolarizabilityprotein-protein association

Identifiers

PMID35994638
PMCPMC9436351
OpenAlexW4293276157

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.