J. Taira et al., NITRIC-OXIDE FORMATION FROM HYDROXYLAMINE BY MYOGLOBIN AND HYDROGEN-PEROXIDE, Biochimica et biophysica acta (G). General subjects, 1336(3), 1997, pp. 502-508
Hydroxylamine (HA), which is a natural product of mammalian cells, has
been shown to possess vasodilatory properties in several model system
s. In this study, HA and methyl-substituted hydroxylamines, N-methylhy
droxylamine (NMHA) and N,N-dimethylhydroxylamine (NDMHA), have been te
sted for their ability to generate free diffusible nitric oxide (NO) i
n the presence of myoglobin (Mb) and hydrogen peroxide. A NO-specific
conversion of nyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (carb
oxy-PTIO) to rboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl (carbo
xy-PTI), measured by electron spin resonance (ESR) spectroscopy, along
with nitrite and nitrate production, was observed for HA but not for
NMHA and NDMHA. ESR measurements at 77 K showed the formation of the f
errous nitrosyl myoglobin, Mb-NO, in the reaction mixtures containing
Mb, H2O2 and HA. Our data also demonstrate that Mb-NO is an end produc
t of the reaction pathway involving Mb, H2O2 and HA, rather than a rea
ction intermediate in the formation of NO. In summary, our results dem
onstrate a possible pathway of NO formation from HA, however, the sign
ificance of this mechanism for bioactivation of HA in vivo is unknown
at the present time. (C) 1997 Elsevier Science B.V.