Abstract
Ni2+, a toxic and carcinogenic pollutant and one of the leading causes of contact dermatitis, is shown to inhibit neuronal nitric oxide synthase (nNOS) in a competitive, reversible manner with respect to the substrate l-arginine (Ki = 30 ± 4 μM). The IC50 values were dependent on calmodulin (CaM) concentration, but proved independent of Ca2+, tetrahydrobiopterin (BH4) and other essential cofactors. Ni2+ also inhibited CaM-dependent cytochrome c reduction, NADPH oxidation, and H2O2 production by nNOS. Overall, the action profile of Ni2+ was suggestive of an unusual, double-acting inhibitor of nNOS affecting l-arginine-binding and Ca2+/CaM-dependent enzyme activation.
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