Evidence map›Paper›PMID 38603772›Full record

ReviewAccounts of chemical research2024

From Ground-State to Excited-State Activation Modes: Flavin-Dependent "Ene"-Reductases Catalyzed Non-natural Radical Reactions.

Haigen Fu, Todd K Hyster

Open access · greenAbstract readReview
In one paragraph

Review in Accounts of chemical research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
24.0field-weighted citation impact, top 1% 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

37 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
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  7. Photoenzymatic CspProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
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  11. Harnessing Photoenzymatic Systems for Intermolecular C-H Fluorination.Angewandte Chemie (International ed. in English) · 2026
    Article
  12. Article
  13. Review
  14. Article
  15. Designing and Engineering Enzymes for New-to-Nature Photobiocatalysis.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  16. New-to-Nature Photoenzymatic Catalysis.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  17. Article
  18. Article
  19. Article
  20. 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

2 authors at 2 institutions in 2 countries.

Haigen FuNHC Key Laboratory of Biotechnology for Microbial Drugs, Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100050, China.
Todd K HysterDepartment of Chemistry, Princeton University, Princeton, New Jersey 08544, United States.ORCID 0000-0003-3560-355X
Chinese Academy of Medical Sciences & Peking Union Medical College · CNPrinceton University · US

Funding

Hyster (Rivas-Souchet) Diversity SupplementR01GM127703 · NIGMS · PRINCETON UNIVERSITY · PI Todd Kurt Hyster · 2018 to 2026
$2.9M
NIGMS NIH HHS R01 GM127703
6 · The paper itself

Abstract

Enzymes are desired catalysts for chemical synthesis, because they can be engineered to provide unparalleled levels of efficiency and selectivity. Yet, despite the astonishing array of reactions catalyzed by natural enzymes, many reactivity patterns found in small molecule catalysts have no counterpart in the living world. With a detailed understanding of the mechanisms utilized by small molecule catalysts, we can identify existing enzymes with the potential to catalyze reactions that are currently unknown in nature. Over the past eight years, our group has demonstrated that flavin-dependent "ene"-reductases (EREDs) can catalyze various radical-mediated reactions with unparalleled levels of selectivity, solving long-standing challenges in asymmetric synthesis.This Account presents our development of EREDs as general catalysts for asymmetric radical reactions. While we have developed multiple mechanisms for generating radicals within protein active sites, this account will focus on examples where flavin mononucleotide hydroquinone (FMN

Indexed as

OxidoreductasesBiocatalysisElectron TransportFlavin MononucleotideFlavinsFree RadicalsHydroquinonesFlavin MononucleotideFlavinsFree RadicalsHydroquinonesOxidoreductases

Identifiers

PMID38603772
PMCPMC11618812
OpenAlexW4394710711

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.