Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Regular Papers
Melanogenesis Inhibition Due to NADH
Francis GARCIA-MOLINAJoseph Louis MUNOZ-MUNOZMary GARCIA-MOLINAPeter Anthony GARCIA-RUIZJoseph TUDELAFrancis GARCÍA-CÁNOVASJoseph Neptune RODRIGUEZ-LOPEZ
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2010 Volume 74 Issue 9 Pages 1777-1787

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Abstract

The effect of NADH on melanogenesis under aerobic conditions involves three types of reaction: (a) acting as tyrosinase substrate (a competitive substrate of L-tyrosine and L-DOPA), (b) irreversible inactivation acting as a suicide substrate of tyrosinase, and (c) non-enzymatic reduction of o-dopaquinone by NADH. Under anaerobic conditions, NADH irreversibly inhibits the enzymatic forms met-tyrosinase and deoxy-tyrosinase. In this paper, we kinetically characterize this coenzyme as it acts as a tyrosinase suicide substrate and propose a kinetic mechanism to explain its oxidation by tyrosinase. In addition, the compound is characterized as an irreversible inhibitor of met-tyrosinase and deoxy-tyrosinase.

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© 2010 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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