Влияние нитрозильных комплексов железа – доноров NO на активность Са2+-АТФазы саркоплазматического ретикулума и фосфодиэстеразы циклического гуанозинмонофосфата

We have studied the influence of iron nitrosyl complexes NO donors of various structural types on the activity of sarcoplasmic reticulum (SR) Ca 2+ -ATPase and cyclic guanosine monophosphate (cGMP) phosphodiesterase (PDE). It is established that iron nitrosyl complexes with organic ligands modulate functions of both enzymes. In particular, these complexes effectively inhibit the hydrolytic and transport functions of SR-Ca 2+ -ATPase (at concentrations within 0.1 – 0.001 mM) and separate the ATP hydrolysis and Ca 2+ ion transport (at concentrations within 0.01 – 0.0001 mM) thus violating the balance of Ca 2+ ions in cells, which influences the thrombogenesis and the adhesion of metastatic cells to capillary endothelium. Compound [Fe(SC(NH 2 ) 2 ) 2 (NO) 2 ] 2 [Fe (S 2 O 3 ) 2 (NO) 4 ] produces incompetent reversible inhibition of SR-Ca 2+ -ATPase function at K i = 0.70×10 –6 M. All iron nitrosyl complexes studied inhibit the activity of cGMP-PDE, which leads to the accumulation of cGMP that is a secondary messenger influencing the antiaggregation effect in living organism. The obtained results suggest that the iron nitrosyl complexes studied can be considered as potential drugs.