Effect of nitroso compounds on Na/K-ATPase

Thiol containing NO.-derivatives were found to inhibit the activity of brain and kidney Na/K-ATPase. S-Nitrosogluthatione demonstrated only minor inhibiting activity, while dinitrosyl iron complexes (DNIC) with cysteine or glutathione were much more effective. Brain Na/K-ATPase is more vulnerable to inhibiting action than kidney Na/K-ATPase. Inhibition of the activity is accompanied by a decrease in amount of protein thiol groups and a change in the substrate dependence curve of the enzyme. Restoration of Na/K-ATPase activity by SH-reagent dithiothreitol or cysteine is accompanied by restoration of SH-groups of the enzyme. This suggests that blockade of SH-groups of Na/K-ATPase is responsible for the inhibition. The possibility that this blockade results in disordering of interprotomer interactions within the oligomeric complexes of Na/K-ATPase is suggested. Possible regulatory meaning of the effect of NO. derivatives is discussed.