Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase.

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.