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Pigment Cell Melanoma Res. 2014 Nov;27(6):1149-53. doi: 10.1111/pcmr.12300. Epub 2014 Sep 3.

Human tyrosinase is able to oxidize both enantiomers of rhododendrol.

Author information

1
Department of Chemistry, Fujita Health University School of Health Sciences, Toyoake, Aichi, Japan.

Abstract

Racemic RS-4-(4-hydroxyphenyl)-2-butanol (rhododendrol, RD) was used as a topical skin-whitening agent until it was recently reported to induce leukoderma. We then showed that oxidation of RD with mushroom tyrosinase rapidly produces RD-quinone, which is quickly converted to RD-cyclic quinone and RD-hydroxy-p-quinone. In this study, we examined whether either or both of the enantiomers of RD can be oxidized by human tyrosinase. Using a chiral HPLC column, racemic RD was resolved optically to R(-)-RD and S(+)-RD enantiomers. In the presence of a catalytic amount of l-dopa, human tyrosinase, which can oxidize l-tyrosine but not d-tyrosine, was found to oxidize both R(-)- and S(+)-RD to give RD-catechol and its oxidation products. S(+)-RD was more effectively oxidized than l-tyrosine, while R(-)-RD was less effective. These results support the notion that the melanocyte toxicity of RD depends on its tyrosinase-catalyzed conversion to toxic quinones and the concomitant production of reactive oxygen species.

KEYWORDS:

human tyrosinase; melanocyte toxicity; rhododendrol; whitening agent

PMID:
25130058
DOI:
10.1111/pcmr.12300
[Indexed for MEDLINE]

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