Evidence map›Paper›PMID 34941416›Full record

ArticleScience (New York, N.Y.)2021

Stereodivergent atom-transfer radical cyclization by engineered cytochromes P450.

Qi Zhou, Michael Chin, Yue Fu, Peng Liu, Yang Yang

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
14.3field-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

69 citing papers in PubMed, 174 citations in OpenAlex.

  1. Design-Evolution Synergy Enables New-to-Nature Enzyme Chemistry.bioRxiv : the preprint server for biology · 2026
    Article
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  11. Asymmetric Ketone Diene Coupling via Stereodivergent Copper Catalysis.Journal of the American Chemical Society · 2026
    Article
  12. Article
  13. Article
  14. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  15. Article
  16. Bimolecular Homolytic Substitution (SACS central science · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Article

9 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Qi ZhouDepartment of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA 93106, USA.ORCID 0000-0003-0577-1595
Michael Chin *Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA 93106, USA.ORCID 0000-0002-8943-7262
Yue Fu *Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Peng LiuDepartment of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.ORCID 0000-0002-8188-632X
Yang YangDepartment of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA 93106, USA.ORCID 0000-0002-4956-2034
University of California, Santa Barbara · USUniversity of Pittsburgh · US

Funding

Computational Models for Reactivity and Selectivity in Transition Metal-Catalyzed Olefin FunctionalizationR35GM128779 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Peng Liu · 2018 to 2026
$2.9M
An Evolvable Metalloenzyme Platform for Stereoselective Radical BiocatalysisR35GM147387 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI Yang Yang · 2022 to 2026
$2.0M
NIGMS NIH HHS R35 GM128779NIGMS NIH HHS R35 GM147387
6 · The paper itself

Abstract

Naturally occurring enzymes can be a source of unnatural reactivity that can be molded by directed evolution to generate efficient biocatalysts with valuable activities. Owing to the lack of exploitable stereocontrol elements in synthetic systems, steering the absolute and relative stereochemistry of free-radical processes is notoriously difficult in asymmetric catalysis. Inspired by the innate redox properties of first-row transition-metal cofactors, we repurposed cytochromes P450 to catalyze stereoselective atom-transfer radical cyclization. A set of metalloenzymes was engineered to impose substantial stereocontrol over the radical addition step and the halogen rebound step in these unnatural processes, allowing enantio- and diastereodivergent radical catalysis. This evolvable metalloenzyme platform represents a promising solution to tame fleeting radical intermediates for asymmetric catalysis.

Indexed as

Protein EngineeringBiocatalysisChemistry Techniques, SyntheticCyclizationCytochrome P-450 Enzyme SystemDirected Molecular EvolutionFree RadicalsMolecular StructureOxidation-ReductionStereoisomerismCytochrome P-450 Enzyme SystemFree Radicals

Identifiers

PMID34941416
PMCPMC9309897
OpenAlexW4200187979

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.