Evidence map›Paper›PMID 31356719›Full record

ReviewAngewandte Chemie (International ed. in English)2019

Site-Selective Functionalization of (sp

Yang Gu, Sean N Natoli, Zhennan Liu, Douglas S Clark, John F Hartwig

Open access · greenAbstract readReview
In one paragraph

Review in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.1field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Exploring LinearJournal of medicinal chemistry · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Chemodivergent C(spNature catalysis · 2023
    Article
  13. Article
  14. Article
  15. Peroxidase Activity of Myoglobin Variants Reconstituted with Artificial Cofactors.Chembiochem : a European journal of chemical biology · 2022
    Article
  16. Review
  17. Article
  18. Review
  19. Directed Evolution of Artificial Metalloenzymes in Whole Cells.Angewandte Chemie (International ed. in English) · 2022
    Article
  20. Assembly and Evolution of Artificial Metalloenzymes withinJournal of the American Chemical Society · 2022
    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

5 authors at 1 institution in 1 country.

Yang GuDepartment of Chemistry, University of California, Berkeley, CA, 94720, USA.
Sean N NatoliDepartment of Chemistry, University of California, Berkeley, CA, 94720, USA.
Zhennan LiuDepartment of Chemistry, University of California, Berkeley, CA, 94720, USA.
Douglas S ClarkDepartment of Chemical and Biomolecular Engineering, University of California, Berkeley, CA, 94720, USA.
John F HartwigDepartment of Chemistry, University of California, Berkeley, CA, 94720, USA.ORCID 0000-0002-4157-468X
Lawrence Berkeley National Laboratory · US

Funding

Expanding Catalytic Amination by Artificial Metalloenzymes through Cofactor Design and Directed EvolutionF32GM126652 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI NATOLI, SEAN NICHOLAS · 2017 to 2019
$118k
NIGMS NIH HHS F32 GM126652U.S. Department of Energy DE-AC02-05CH11231
6 · The paper itself

Abstract

The selective functionalization of one C-H bond over others in nearly identical steric and electronic environments can facilitate the construction of complex molecules. We report site-selective functionalizations of C-H bonds, differentiated solely by remote substituents, catalyzed by artificial metalloenzymes (ArMs) that are generated from the combination of an evolvable P450 scaffold and an iridium-porphyrin cofactor. The generated systems catalyze the insertion of carbenes into the C-H bonds of a range of phthalan derivatives containing substituents that render the two methylene positions in each phthalan inequivalent. These reactions occur with site-selectivity ratios of up to 17.8:1 and, in most cases, with pairs of enzyme mutants that preferentially form each of the two constitutional isomers. This study demonstrates the potential of abiotic reactions catalyzed by metalloenzymes to functionalize C-H bonds with site selectivity that is difficult to achieve with small-molecule catalysts.

Indexed as

CatalysisIridiumMetalloproteinsPorphyrinsStereoisomerismIridiumMetalloproteinsPorphyrinsartificial metalloenzymesbiocatalysisC−H functionalizationP450 enzymesporphyrins

Identifiers

PMID31356719
PMCPMC6759379
OpenAlexW2965796251

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.