Abstract
We report here our studies of new nitrosyl complexes of iron of the cationic type - [Fe2(SR′)2(NO)4]2+ with R′ = cysteamine and penicillamine - and of the neutral type - [Fe2(SR″)2(NO)4]0 with R″ = benzthiazoline – on the enzymatic activity of hydrolases – cyclic guanosine monophosphate phosphodiesterase (PDEcGMP) and sarcoplasmic reticulum Ca2+-Mg2+-dependent ATPase (SR-Ca2+-ATPase). All the complexes studied were found to be modulators of both enzymes. They produced weak inhibition of PDEcGMP activity and marked inhibition of active transport by SR Ca2+-ATPase. While having virtually no effect on the hydrolytic center of SR Ca2+-ATPase, the active transport of calcium was completely blocked over the concentration range 1 μM – 0.1 mM, with uncoupling of the hydrolytic and transport functions of this enzyme. This suggests that these complexes can induce structural-functional changes in SR Ca2+-ATPase at concentrations corresponding to an enzyme:inhibitor ratio of 1:1, which is consistent with the antimetastatic action of these compounds.
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