The effect of NADH on melanogenesis under aerobic conditions involves three types of reaction: (a) acting as tyrosinase substrate (a competitive substrate of Ltyrosine and L-DOPA), (b) irreversible inactivation acting as a suicide substrate of tyrosinase, and (c) nonenzymatic 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 deoxytyrosinase.