Evidence map›Paper›PMID 24567729›Full record

ReviewFrontiers in microbiology2014

Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications.

Romina D Ceccoli, Dario A Bianchi, Daniela V Rial

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 57 citations in OpenAlex.

  1. Surveying aIranian journal of microbiology · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Mechanism UnderlyingToxins · 2023
    Article
  6. Article
  7. Article
  8. Uncovering the Biotechnological Importance ofFoods (Basel, Switzerland) · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  13. Article
  14. Characterization ofFrontiers in genetics · 2020
    Article
  15. Article
  16. Review
  17. Mining the Genome ofFrontiers in microbiology · 2018
    Article
  18. Article
  19. Regulated methionine oxidation by monooxygenases.Free radical biology & medicine · 2017
    Review
  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

3 authors at 1 institution in 1 country.

Romina D CeccoliÁrea Biología Molecular, Departamento de Ciencias Biológicas, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario CONICET, Rosario, Argentina.
Dario A BianchiInstituto de Química Rosario (IQUIR, CONICET-UNR), Área Análisis de Medicamentos, Departamento de Química Orgánica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario Rosario, Argentina.
Daniela V RialÁrea Biología Molecular, Departamento de Ciencias Biológicas, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario CONICET, Rosario, Argentina.
National University of Rosario · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

External flavoprotein monooxygenases comprise a group of flavin-dependent oxidoreductases that catalyze the insertion of one atom of molecular oxygen into an organic substrate and the second atom is reduced to water. These enzymes are involved in a great number of metabolic pathways both in prokaryotes and eukaryotes. Flavoprotein monooxygenases have attracted the attention of researchers for several decades and the advent of recombinant DNA technology caused a great progress in the field. These enzymes are subjected to detailed biochemical and structural characterization and some of them are also regarded as appealing oxidative biocatalysts for the production of fine chemicals and valuable intermediates toward active pharmaceutical ingredients due to their high chemo-, stereo-, and regioselectivity. Here, we review the most representative reactions catalyzed both in vivo and in vitro by prototype flavoprotein monooxygenases, highlighting the strategies employed to produce them recombinantly, to enhance the yield of soluble proteins, and to improve cofactor regeneration in order to obtain versatile biocatalysts. Although we describe the most outstanding features of flavoprotein monooxygenases, we mainly focus on enzymes that were cloned, expressed and used for biocatalysis during the last years.

Indexed as

Baeyer–Villiger oxidationbiocatalysisbiooxidationsepoxidationflavoprotein monooxygenasehydroxylationrecombinant biocatalystsulfoxidation

Identifiers

PMID24567729
PMCPMC3915288
OpenAlexW2000518729

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.