Evidence map›Paper›PMID 29719099›Full record

ArticleAngewandte Chemie (International ed. in English)2018

An Artificial Heme Enzyme for Cyclopropanation Reactions.

Lara Villarino, Kathryn E Splan, Eswar Reddem, Lur Alonso-Cotchico, Cora Gutiérrez de Souza, Agustí Lledós, Jean-Didier Maréchal, Andy-Mark W H Thunnissen, Gerard Roelfes

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Reprogramming NAD(P)Angewandte Chemie (International ed. in English) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Unlocking New Reactivities in Enzymes by Iminium Catalysis.Angewandte Chemie (International ed. in English) · 2022
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Catalytic Synthesis of 1Journal of the American Chemical Society · 2021
    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

9 authors.

Lara VillarinoStratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, The Netherlands.ORCID 0000-0003-4728-2001
Kathryn E SplanDepartment of Chemistry, Macalester College, 1600 Grand Avenue, Saint Paul, MN, 55105, USA.
Eswar ReddemStratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, The Netherlands.
Lur Alonso-CotchicoDepartament de Química, Universitat Autònoma de Barcelona, Edifici C.n., 08193 Cerdanyola del Vallés, Barcelona, Spain.
Cora Gutiérrez de SouzaStratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, The Netherlands.
Agustí LledósDepartament de Química, Universitat Autònoma de Barcelona, Edifici C.n., 08193 Cerdanyola del Vallés, Barcelona, Spain.ORCID 0000-0001-7909-422X
Jean-Didier MaréchalDepartament de Química, Universitat Autònoma de Barcelona, Edifici C.n., 08193 Cerdanyola del Vallés, Barcelona, Spain.ORCID 0000-0002-8344-9043
Andy-Mark W H ThunnissenGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, The Netherlands.
Gerard RoelfesStratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, The Netherlands.ORCID 0000-0002-0364-9564

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An artificial heme enzyme was created through self-assembly from hemin and the lactococcal multidrug resistance regulator (LmrR). The crystal structure shows the heme bound inside the hydrophobic pore of the protein, where it appears inaccessible for substrates. However, good catalytic activity and moderate enantioselectivity was observed in an abiological cyclopropanation reaction. We propose that the dynamic nature of the structure of the LmrR protein is key to the observed activity. This was supported by molecular dynamics simulations, which showed transient formation of opened conformations that allow the binding of substrates and the formation of pre-catalytic structures.

Indexed as

CatalysisCrystallography, X-RayCyclopropanesDrug Resistance, MultipleEnzymesHemeHydrophobic and Hydrophilic InteractionsMolecular Dynamics SimulationProtein ConformationSpectrophotometry, UltravioletSubstrate SpecificitycyclopropaneCyclopropanesEnzymesHemeartificial metalloenzymesbiocatalysiscarbenesenzyme designheme enzymes

Identifiers

PMID29719099
PMCPMC6033091

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.