Evidence map›Paper›PMID 40557563›Full record

ArticleChemistryOpen2025

Challenges in Mechanistic Investigation of a Flexible Aminocatalyst as Demonstrated through Enamine Formation.

Irina Osadchuk, Tõnis Kanger

Abstract read
In one paragraph

Article in ChemistryOpen, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Irina OsadchukDepartment of Chemistry and Biotechnology, Tallinn University of Technology, Akadeemia tee 15, 12618, Tallinn, Estonia.ORCID https://orcid.org/0000-0003-1640-4328
Tõnis KangerDepartment of Chemistry and Biotechnology, Tallinn University of Technology, Akadeemia tee 15, 12618, Tallinn, Estonia.ORCID https://orcid.org/0000-0001-5339-9682

Funding

Estonian Academy of Sciences ETR22017Estonian Ministry of Education and Research PRG1031
6 · The paper itself

Abstract

Asymmetric catalysis has become a prominent topic in synthesis over recent decades. Conformational changes in the catalyst core play a significant role in the reaction, determining both its rate and selectivity. This article presents computational studies of enamine formation from cyclohexanone and the tripeptide catalyst Phe-Lys-Phe and considers challenges related to conformational search and the selection of an appropriate level of theory for studying flexible catalysts. This also demonstrates the importance of selecting the initial model system and how reducing the system under study or including the entire system in the model can impact the study's outcome. Furthermore, incorporating a water molecule into the model system significantly reduces the energy of proton transfer. Finally, the catalyst's ability to reorganize plays an important role, since it allows the energy of the transition states to be reduced. Thus, this shows that an alternative reaction pathway is more favorable than the one initially found, and the catalyst's flexibility allows and contributes its conformations to vary at different stages of the reaction.

Indexed as

computational chemistryconformational analysesnoncovalent interactionsorganocatalysisreaction mechanisms

Identifiers

PMID40557563
PMCPMC12409831

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.