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J Biol Chem, Vol. 273, Issue 41, 26528-26533, October 9, 1998
From the Division of Critical Care Medicine, Children's Hospital
Medical Center, Cincinnati, Ohio 45229
Nitric oxide (NO·) is a naturally
occurring toxin that some organisms adaptively resist. In aerobic or
anaerobic Escherichia coli, low levels of NO·
exposure inactivated the NO·-sensitive citric acid cycle enzyme
aconitase, and inactivation was more effective when the adaptive
synthesis of NO·-defensive proteins was blocked with
chloramphenicol. Protection of aconitase in aerobically grown E. coli was dependent upon O2, was potently inhibited by
cyanide, and was correlated with an induced rate of cellular NO·
consumption. Constitutive and adaptive cellular NO· consumption
in aerobic cells was also dependent upon O2 and inhibited by cyanide. Exposure of aerobic cells to NO· accordingly
elevated the activity of the O2-dependent and
cyanide-sensitive NO· dioxygenase (NOD). Anaerobic E. coli exposed to NO· or nitrate induced a modest
O2-independent and cyanide-resistant NO·-metabolizing activity and a more robust
O2-stimulated cyanide-sensitive activity. The latter
activity was attributed to NOD. The results support a role for NOD in
the aerobic detoxification of NO· and suggest functions for NOD
and a cyanide-resistant NO· scavenging activity in anaerobic
cells.
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