Evidence map›Paper›PMID 41011567›Full record

ArticleMolecules (Basel, Switzerland)2025

The Activation of Cytochrome P450 2C9 Is Facilitated by the Coenzyme Forms of Vitamin B2.

Polina I Koroleva, Alexey V Kuzikov, Andrei A Gilep, Sergey V Ivanov, Alexander I Archakov, Victoria V Shumyantseva

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 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

6 authors.

Polina I KorolevaInstitute of Biomedical Chemistry, Pogodinskaya Street, 10, Build 8, 119121 Moscow, Russia.
Alexey V KuzikovInstitute of Biomedical Chemistry, Pogodinskaya Street, 10, Build 8, 119121 Moscow, Russia.ORCID 0000-0002-8772-3214
Andrei A GilepInstitute of Biomedical Chemistry, Pogodinskaya Street, 10, Build 8, 119121 Moscow, Russia.ORCID 0000-0002-3621-6482
Sergey V IvanovInstitute of Biomedical Chemistry, Pogodinskaya Street, 10, Build 8, 119121 Moscow, Russia.ORCID 0000-0003-0438-9108
Alexander I ArchakovInstitute of Biomedical Chemistry, Pogodinskaya Street, 10, Build 8, 119121 Moscow, Russia.
Victoria V ShumyantsevaInstitute of Biomedical Chemistry, Pogodinskaya Street, 10, Build 8, 119121 Moscow, Russia.ORCID 0000-0002-1509-7218

Funding

Ministry of Science and Higher Education of the Russian Federation 075-15-2024-643
6 · The paper itself

Abstract

The activity of cytochrome P450 enzymes decreases in older adults, which can lead to toxic effects from polypharmacy. Cytochromes P450 are the most significant enzymes involved in the metabolism of foreign compounds, including pharmaceutical substances. Vitamin B2, or riboflavin (RF), is a potent antioxidant that is vital for the body and participates in numerous enzyme-catalyzed redox reactions. RF is phosphorylated intracellularly to form flavin mononucleotide (FMN), which is further metabolized into flavin adenine dinucleotide (FAD). The active site of the NADPH-dependent cytochrome P450 reductase (CPR), a redox partner of CYP enzymes, is necessary for the catalytic functions of cytochromes P450. The active site of reductase is a complex formed by two types of vitamin B2, such as flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN). In our study, we investigated the impact of the phosphorylated form of vitamin B2, FAD, and FMN on the catalytic activity of cytochrome P450 2C9 (CYP2C9) towards non-steroidal anti-inflammatory medications diclofenac and naproxen. It was shown that FAD significantly enhanced the catalytic efficiency of CYP2C9. The 4-hydroxylation of diclofenac was enhanced by 148 ± 10%. The O-demethylation of naproxen showed an increase of 120 ± 14%. Based on these data, we can assume that intake of vitamin B2 (riboflavin) improves catalytic efficiency of CYP2C9. This finding is essential for the modulation of catalytic activity of CYP2C9. The proposed electroanalytic approach is a sensitive and robust method for drug metabolism assay.

Indexed as

CoenzymesCytochrome P-450 CYP2C9RiboflavinCatalytic DomainDiclofenacEnzyme ActivationFlavin-Adenine DinucleotideFlavin MononucleotideHumansHydroxylationNaproxenOxidation-ReductionCoenzymesCYP2C9 protein, humanCytochrome P-450 CYP2C9DiclofenacFlavin-Adenine DinucleotideFlavin MononucleotideNaproxenRiboflavinCYP2C9diclofenacelectrochemical analysiselectron transferenzymatic assaynaproxenprotective propertiesriboflavin

Identifiers

PMID41011567
PMCPMC12472352

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Registered trials

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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.