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- W2034672404 abstract "Nitric oxide synthase (NOS: EC 1.14.13.39) catalyzes l-arginine oxidation to generate nitric oxide (NO) and l-citrulline. Recently, 7-ethoxyresorufin (7-ER), a specific substrate of cytochrome P-4501A1, was used as a cytochrome P-450 inhibitor to study the mechanism underlying the vasodilatation caused by some drugs, and was suggested to inhibit nitric oxide-mediated relaxation. Herein we demonstrate that 7-ER inhibits NO synthesis by uncoupling neuronal nitric oxide synthase (nNOS). 7-ER is a noncompetitive inhibitor of nNOS with respect to l-arginine with a Ki value of 0.76 ± 0.06 μM. The decrease in NO formation is inversely correlated with an increase in NADPH oxidation. 7-ER binds to nNOS with a Km value of 0.68 ± 0.07 μM, as calculated from the nNOS-dependent NADPH oxidation in the absence of l-arginine. nNOS catalyzes the reduction of 7-ER at the expense of NADPH. The flavoprotein inhibitor, diphenyleneiodonium chloride (100 μM), completely inhibited nNOS-dependent 7-ER reduction. While nitro-L-arginine (1 mM) and NG-nitro-L-arginine methyl ester (1 mM), specific inhibitors of nNOS, and phenylisocyanide (0.1mM), a specific heme iron ligand, did not affect the reduction of 7-ER. These results indicate that the reductase domain, but not the oxygenase domain, of nNOS is involved in the reduction of 7-ER. 7-ER uncouples nNOS, shunting electrons from the reductase domain to the oxygenase domain of the enzyme. As a consequence, NO synthesis is inhibited." @default.
- W2034672404 created "2016-06-24" @default.
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- W2034672404 date "1999-08-01" @default.
- W2034672404 modified "2023-09-25" @default.
- W2034672404 title "Neuronal nitric oxide synthase catalyzes the reduction of 7-ethoxyresorufin" @default.
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- W2034672404 doi "https://doi.org/10.1016/s0024-3205(99)00361-6" @default.
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