Evidence map›Paper›PMID 34368824›Full record

ReviewChemical Society reviews2021

Halogenases: a palette of emerging opportunities for synthetic biology-synthetic chemistry and C-H functionalisation.

Charlotte Crowe, Samuel Molyneux, Sunil V Sharma, Ying Zhang, Danai S Gkotsi, Helen Connaris, Rebecca J M Goss

Open access · hybridAbstract readReview
In one paragraph

Review in Chemical Society reviews, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.6field-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

52 citing papers in PubMed, 121 citations in OpenAlex.

  1. Net fluorine atom transfer from the perspective of a PCET chemist.Chemical communications (Cambridge, England) · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mapping of the viral shunt across widespread coccolithophore blooms using metabolic biomarkers.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Examining Pseudohalide (NJournal of inorganic biochemistry · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Sequential Reconstruction of Calicheamicin γAngewandte Chemie (International ed. in English) · 2025
    Article
  19. Article
  20. 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

7 authors at 1 institution in 1 country.

Charlotte CroweSchool of Chemistry, and BSRC, University of St Andrews, North Haugh, St Andrews KY16 9ST, UK. rjmg@st-andrews.ac.uk.
Samuel Molyneux
Sunil V Sharma
Ying Zhang
Danai S Gkotsi
Helen Connaris
Rebecca J M Goss
University of St Andrews · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzymatic generation of carbon-halogen bonds is a powerful strategy used by both nature and synthetic chemists to tune the bioactivity, bioavailability and reactivity of compounds, opening up the opportunity for selective C-H functionalisation. Genes encoding halogenase enzymes have recently been shown to transcend all kingdoms of life. These enzymes install halogen atoms into aromatic and less activated aliphatic substrates, achieving selectivities that are often challenging to accomplish using synthetic methodologies. Significant advances in both halogenase discovery and engineering have provided a toolbox of enzymes, enabling the ready use of these catalysts in biotransformations, synthetic biology, and in combination with chemical catalysis to enable late stage C-H functionalisation. With a focus on substrate scope, this review outlines the mechanisms employed by the major classes of halogenases, while in parallel, it highlights key advances in the utilisation of the combination of enzymatic halogenation and chemical catalysis for C-H activation and diversification.

Indexed as

HalogenationSynthetic BiologyCatalysis

Identifiers

PMID34368824
PMCPMC8407142
OpenAlexW3191820221

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.