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Inactivation of tyrosinase photoinduced by pterin.

Abstract：

:Tyrosinase catalyzes in mammals the first and rate-limiting step in the biosynthesis of the melanin, the main pigment of the skin. Pterins, heterocyclic compounds able to photoinduce oxidation of DNA and its components, accumulate in the skin of patients suffering from vitiligo, a chronic depigmentation disorder in which the protection against UV radiation fails due to the lack of melanin. Aqueous solutions of tyrosinase were exposed to UV-A irradiation (350 nm) in the presence of pterin, the parent compound of oxidized pterins, under different experimental conditions. The enzyme activity in the irradiated solutions was determined by spectrophotometry and HPLC. In this work, we present data that demonstrate unequivocally that the enzyme is photoinactivated by pterin. The mechanism of the photosensitized process involves an electron transfer from tyrosinase to the triplet excited state of pterin, formed after UV-A excitation of pterin. The biological implications of the results are discussed.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Laura Dántola M,Gojanovich AD,Thomas AH

doi

10.1016/j.bbrc.2012.06.155

subject

Has Abstract

pub_date

2012-08-03 00:00:00

pages

568-72

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(12)01267-3

journal_volume

424

pub_type

杂志文章

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