Evidence map›Paper›PMID 36468873›Full record

ArticleAngewandte Chemie (International ed. in English)2023

Aerobic C-N Bond Formation through Enzymatic Nitroso-Ene-Type Reactions.

Christina Jäger, Mona Haase, Katja Koschorreck, Vlada B Urlacher, Jan Deska

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Peroxidase-induced C-N bond formationGreen chemistry : an international journal and green chemistry resource : GC · 2023
    Article
  5. Aerobic C-N Bond Formation through Enzymatic Nitroso-Ene-Type Reactions.Angewandte Chemie (International ed. in English) · 2023
    Article
  6. 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.

Christina JägerUniversity of Helsinki, Department of Chemistry, A.I. Virtasen aukio 1, 00560, Helsinki, Finland.
Mona HaaseAalto University, Department of Chemistry, Kemistintie 1, 02150, Espoo, Finland.
Katja KoschorreckHeinrich-Heine-Universität Düsseldorf, Universitätsstr. 1, 40225, Düsseldorf, Germany.
Vlada B UrlacherHeinrich-Heine-Universität Düsseldorf, Universitätsstr. 1, 40225, Düsseldorf, Germany.ORCID 0000-0003-1312-4574
Jan DeskaUniversity of Helsinki, Department of Chemistry, A.I. Virtasen aukio 1, 00560, Helsinki, Finland.ORCID 0000-0003-4622-2365

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biocatalytic oxidation of acylated hydroxylamines enables the direct and selective introduction of nitrogen functionalities by activation of allylic C-H bonds. Utilizing either laccases or an oxidase/peroxidase couple for the formal dehydrogenation of N-hydroxycarbamates and hydroxamic acids with air as the terminal oxidant, acylnitroso species are generated under particularly mild aqueous conditions. The reactive intermediates undergo C-N bond formation through an ene-type mechanism and provide high yields both in intramolecular and intermolecular enzymatic aminations. Investigations on different pathways of the two biocatalytic systems and labelling studies provide more insight into this unprecedented promiscuity of classical oxidoreductases as catalysts for nitroso-based transformations.

Indexed as

OxidantsOxidoreductasesAminationBiocatalysisCatalysisOxidation-ReductionOxidantsOxidoreductasesAminationBiocatalysisCyclizationEne ReactionHeterocycles

Identifiers

PMID36468873
PMCPMC10107922

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.