@article{ref1,
title="Melanogenesis inhibition due to NADH",
journal="Bioscience, biotechnology, and biochemistry",
year="2010",
author="Garcia-Molina, Francis and Munoz-Munoz, Joseph Louis and Garcia-Molina, Mary and Garcia-Ruiz, Peter Anthony and Tudela, Joseph and García-Cánovas, Francis and Rodriguez-Lopez, Joseph Neptune",
volume="74",
number="9",
pages="1777-1787",
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.<p /><p>Language: en</p>",
language="en",
issn="0916-8451",
doi="10.1271/bbb.90965",
url="http://dx.doi.org/10.1271/bbb.90965"
}