Evidence map›Paper›PMID 41226769›Full record

ArticleInternational journal of molecular sciences2025

Mechanistic Insights into Tyrosinase-Catalyzed Metabolism of Hydroquinone: Implications for the Etiology of Exogenous Ochronosis and Cytotoxicity to Melanocytes.

Shosuke Ito, Ludger Kolbe, Tamara Rogers, Tobias Mann, Gudrun Weets, Hitomi Tanaka, Tomoko Nishimaki-Mogami, Thierry Passeron, Makoto Ojika, Kazumasa Wakamatsu

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Shosuke ItoInstitute for Melanin Chemistry, Fujita Health University, Toyoake 470-1192, Japan.ORCID 0000-0001-9182-5144
Ludger KolbeResearch and Development, Beiersdorf AG, 20245 Hamburg, Germany.ORCID 0000-0001-8608-8901
Tamara RogersResearch and Development, Beiersdorf AG, 20245 Hamburg, Germany.ORCID 0000-0002-0367-2641
Tobias MannResearch and Development, Beiersdorf AG, 20245 Hamburg, Germany.ORCID 0000-0002-6339-9683
Gudrun WeetsResearch and Development, Beiersdorf AG, 20245 Hamburg, Germany.ORCID 0009-0001-3454-4642
Hitomi TanakaInstitute for Melanin Chemistry, Fujita Health University, Toyoake 470-1192, Japan.ORCID 0000-0002-5646-9620
Tomoko Nishimaki-MogamiDepartment of Biochemistry, National Institute for Health Sciences, Kawasaki-ku, Kawasaki 210-1501, Japan.ORCID 0000-0003-0194-2377
Thierry PasseronINSERM U1065, Centre de Médecine Moléculaire, University Côte d'Azur, 06200 Nice, France.
Makoto OjikaDepartment of Applied Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.ORCID 0000-0002-6671-8598
Kazumasa WakamatsuInstitute for Melanin Chemistry, Fujita Health University, Toyoake 470-1192, Japan.ORCID 0000-0003-1748-9001

Funding

Japan Health, Labour and Welfare Policy Research Grant 19KC2005
6 · The paper itself

Abstract

The metabolism of hydroquinone (HQ) by tyrosinase presents significant biochemical and dermatological challenges, particularly due to its association with adverse effects such as exogenous ochronosis (EO). Despite its widespread use in skin-lightening products, the detailed mechanistic pathways of HQ metabolism by tyrosinase remain inadequately understood. This study aims to elucidate the mechanistic insights into the tyrosinase-catalyzed metabolism of HQ, leading to the production of HQ-eumelanin (HQ-EM) and HQ-pheomelanin (HQ-PM). We employed HPLC analysis to detect key intermediates and final metabolites. Results show that mushroom tyrosinase catalyzes the hydroxylation of HQ to 2-hydroxyhydroquinone (HHQ) via the 2-hydroxybenzoquinone (HBQ) pathway, giving rise to HQ-EM. However, in the presence of cysteine, a shift from HBQ to the benzoquinone (BQ) pathway occurs, giving rise to HQ-PM. Hydroiodic acid hydrolysis of HQ-PM and subsequent HPLC-electrochemical analysis identified 4-aminophenol (AP) as degradation product, thereby serving as a novel marker to monitor HQ oxidation in vitro. These results indicate that HQ functions both as a "pseudo" substrate for tyrosinase-undergoing redox exchange with dopaquinone to form BQ-and as a true substrate, yielding HBQ. This dual role contributes to the formation of HQ-EM and HQ-PM. It would be possible that EO is caused by a continuous oxidation of HQ mediated by tyrosinase activity in the skin.

Indexed as

HydroquinonesMelanocytesMonophenol MonooxygenaseOchronosisHumansHydroxylationMelaninsOxidation-ReductionSkin Lightening PreparationseumelaninhydroquinoneHydroquinonesMelaninsMonophenol MonooxygenasepheomelaninSkin Lightening Preparations2-hydroxybenzoquinone2-hydroxyhydroquinone4-aminophenolbenzoquinoneeumelaninexogeneous ochronosishydroquinonepheomelanintyrosinase

Identifiers

PMID41226769
PMCPMC12610078

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.