Compounds > 1-1-diethyl-2-hydroxy-2-nitrosohydrazine

1-1-diethyl-2-hydroxy-2-nitrosohydrazine and 4-(2-pyridylazo)resorcinol

1-1-diethyl-2-hydroxy-2-nitrosohydrazine has been researched along with 4-(2-pyridylazo)resorcinol* in 1 studies

Other Studies

1 other study(ies) available for 1-1-diethyl-2-hydroxy-2-nitrosohydrazine and 4-(2-pyridylazo)resorcinol

Article	Year
Oxidation and nitrosation in the nitrogen monoxide/superoxide system. The Journal of biological chemistry, 2002, Apr-05, Volume: 277, Issue:14 Based on the previous report of McCord and co-workers (Crow, J. P., Beckman, J. S., and McCord, J. M. (1995) Biochemistry 34, 3544-3552), the zinc dithiolate active site of alcohol dehydrogenase (ADH) has been studied as a target for cellular oxidants. In the nitrogen monoxide ((NO)/superoxide (O(2)) system, an equimolar generation of both radicals under peroxynitrite (PN) formation led to rapid inactivation of ADH activity, whereas hydrogen peroxide and ( small middle dot)NO alone reacted too slowly to be of physiological significance. 3-Morpholino sydnonimine inactivated the enzyme with an IC(50) value of 250 nm; the corresponding values for PN, hydrogen peroxide, and (NO) were 500 nm, 50 microm, and 200 microm. When superoxide was generated at low fluxes by xanthine oxidase, it was quite effective in ADH inactivation (IC(50) (XO) approximately 1 milliunit/ml). All inactivations were accompanied by zinc release and disulfide formation, although no strict correlation was observed. From the two zinc thiolate centers, only the zinc Cys(2)His center released the metal by oxidants. The zinc Cys(4) center was also oxidized, but no second zinc atom could be found with 4-(2-pyridylazo)resorcinol (PAR) as a chelating agent except under denaturing conditions. Surprisingly, the oxidative actions of PN were abolished by a 2-3-fold excess of ()NO under generation of a nitrosating species, probably dinitrogen trioxide. We conclude that in cellular systems, low fluxes of ()NO and O(2) generate peroxynitrite at levels effective for zinc thiolate oxidations, facilitated by the nucleophilic nature of the complexed thiolate group. With an excess of ()NO, the PN actions are blocked, which may explain the antioxidant properties of ()NO and the mechanism of cellular S-nitrosations. Topics: Animals; Biochemical Phenomena; Biochemistry; Cattle; Chelating Agents; Chromatography, High Pressure Liquid; Chromogenic Compounds; Disulfides; Dose-Response Relationship, Drug; Free Radicals; Hydrazines; Hydrogen Peroxide; Models, Chemical; Molsidomine; Nitric Oxide; Nitric Oxide Donors; Nitrogen; Nitrogen Oxides; Oxygen; Peroxynitrous Acid; Protein Binding; Resorcinols; Spectrophotometry; Spectrum Analysis, Raman; Spermine; Sulfhydryl Compounds; Superoxides; Time Factors; Ultraviolet Rays; Xanthine Oxidase; Zinc	2002

Article

Year

Oxidation and nitrosation in the nitrogen monoxide/superoxide system.

The Journal of biological chemistry, 2002, Apr-05, Volume: 277, Issue:14

Based on the previous report of McCord and co-workers (Crow, J. P., Beckman, J. S., and McCord, J. M. (1995) Biochemistry 34, 3544-3552), the zinc dithiolate active site of alcohol dehydrogenase (ADH) has been studied as a target for cellular oxidants. In the nitrogen monoxide ((*NO)/superoxide (O(2)) system, an equimolar generation of both radicals under peroxynitrite (PN) formation led to rapid inactivation of ADH activity, whereas hydrogen peroxide and ( small middle dot)NO alone reacted too slowly to be of physiological significance. 3-Morpholino sydnonimine inactivated the enzyme with an IC(50) value of 250 nm; the corresponding values for PN, hydrogen peroxide, and (*NO) were 500 nm, 50 microm, and 200 microm. When superoxide was generated at low fluxes by xanthine oxidase, it was quite effective in ADH inactivation (IC(50) (XO) approximately 1 milliunit/ml). All inactivations were accompanied by zinc release and disulfide formation, although no strict correlation was observed. From the two zinc thiolate centers, only the zinc Cys(2)His center released the metal by oxidants. The zinc Cys(4) center was also oxidized, but no second zinc atom could be found with 4-(2-pyridylazo)resorcinol (PAR) as a chelating agent except under denaturing conditions. Surprisingly, the oxidative actions of PN were abolished by a 2-3-fold excess of (*)NO under generation of a nitrosating species, probably dinitrogen trioxide. We conclude that in cellular systems, low fluxes of (*)NO and O(2) generate peroxynitrite at levels effective for zinc thiolate oxidations, facilitated by the nucleophilic nature of the complexed thiolate group. With an excess of (*)NO, the PN actions are blocked, which may explain the antioxidant properties of (*)NO and the mechanism of cellular S-nitrosations.

Topics: Animals; Biochemical Phenomena; Biochemistry; Cattle; Chelating Agents; Chromatography, High Pressure Liquid; Chromogenic Compounds; Disulfides; Dose-Response Relationship, Drug; Free Radicals; Hydrazines; Hydrogen Peroxide; Models, Chemical; Molsidomine; Nitric Oxide; Nitric Oxide Donors; Nitrogen; Nitrogen Oxides; Oxygen; Peroxynitrous Acid; Protein Binding; Resorcinols; Spectrophotometry; Spectrum Analysis, Raman; Spermine; Sulfhydryl Compounds; Superoxides; Time Factors; Ultraviolet Rays; Xanthine Oxidase; Zinc

2002