Evidence map›Paper›PMID 39990936›Full record

ReviewACS bio & med chem Au2025

Mechanistic Perspective on C-N and C-S Bond Construction Catalyzed by Cytochrome P450 Enzymes.

Tai-Ping Zhou, Yakun Fan, Jinyan Zhang, Binju Wang

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in ACS bio & med chem Au, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

4 authors.

Tai-Ping ZhouState Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.
Yakun FanState Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.
Jinyan ZhangState Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.
Binju WangState Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.ORCID https://orcid.org/0000-0002-3353-9411

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochrome P450 enzymes catalyze a large number of oxidative transformations that are responsible for natural product synthesis. Recent studies have revealed their unique ability to catalyze the formation of C-N and C-S bonds, broadening their biosynthetic applications. However, the enzymatic mechanisms behind these reactions are still unclear. This review focuses on theoretical insights into the mechanisms of P450-catalyzed C-N and C-S bond formation. The key roles of the conformational dynamics of substrate radicals, influenced by the enzyme environment, in modulating selectivity and reactivity are highlighted. Understanding these reaction mechanisms offers valuable guidance for P450 enzyme engineering and the design of biosynthetic applications.

Identifiers

PMID39990936
PMCPMC11843346

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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.