Effects of Covalent Conjugates of Fullerene Derivatives with Xanthene Dyes on Activity of Ca-ATPase of the Sarcoplasmic Reticulum.

The effects of the newly synthesized covalent conjugates of water-soluble fullerene derivatives (WSFD) with xanthene dyes: polyanionic WSFD-fluorescein (1), polycationic WSFD-fluorescein (2), polyanionic WSFD-eosin (3), and polyanionic WSFD (4), polycationic WSFD (5), fluorescein (6) and eosin (7), on activity of the membrane-bound Ca-ATPase of the sarcoplasmic reticulum (SR Ca-ATPase) were studied. Compounds 1, 3, 4, 6, and 7 inhibit the hydrolytic function of the enzyme, the inhibition constants for these compounds are Ki=1.3×10 M (1), Ki=4.

The Effect of Nitroxyalkyl Succinimides on Activity of Cyclic Guanosine Monophosphate Phosphodiesterase.

The effect of N-nitroxymethyl succinimide (1), N-(2-nitroxyethyl) succinimide (2) and N-(3-nitroxypropyl) succinimide (3) on enzymatic activity of cyclic guanosine monophosphate (cGMP) phosphodiesterase was studied and crystal structure of compound (2) was determined. It was shown that all studied N-nitroxy succinimides inhibited cGMP phosphodiesterase in a concentration range of 0.1-0.

Action of Iron Nitrosyl Complexes, NO Donors, on the Activity of Sarcoplasmic Reticulum Ca-ATPase and Cyclic Guanosine Monophosphate Phosphodiesterase.

The effect of iron nitrosyl complexes, NO donors, of a general formula [Fe(L)(NO)] with functional sulfur-containing ligands (L-3-nitro-phenol-2-yl, 4-nitro-phenol-2-yl, or 1-methyl-tetrazol-5-yl) on the activity of sarcoplasmic reticulum Ca-ATPase and cyclic guanosine monophosphate phosphodiesterase (cGMP PDE) was studied. The test complexes uncoupled the hydrolytic and transport functions of Ca- ATPase, thus disturbing the balance of Ca ions in cells, which may affect the formation of thrombi and adhesion of metastatic cells to the endothelium of capillaries. They also inhibited the activity of cGMP PDE, thereby contributing to the accumulation of the second messenger cGMP.

Effects of Fullerene Derivatives on Activity of Ca-ATPase of the Sarcoplasmic Reticulum and cGMP Phosphodiesterase.

We studied the effects of new water-soluble polysubstituted fullerene C60 (PFD) derivatives on activity of Ca-Mg ATPase of the sarcoplasmic reticulum and cGMP phosphodiesterase. All examined fullerene derivatives inhibited activity of both enzymes. For instance, PFD-I, PFD-II, PFD-III, PFD-V, PFD-IX, PFD-X, and PFD-XI in a concentration of 5×10 M completely inhibited hydrolytic and transport functions of Ca-ATPase.

Effects of Nitrosyl Iron Complexes with Thiocarbamide and Its Aliphatic Derivatives on Activities of Ca-ATPase of Sarcoplasmic Reticulum and cGMP Phosphodiesterase.

We studied the effects of water-soluble cationic dinitrosyl iron complexes with thiocarbamide and its aliphatic derivatives, new synthetic analogs of natural NO donors, active centers of nitrosyl [1Fe-2S]proteins, on activities of Ca-ATPase of sarcoplasmic reticulum and cGMP phosphodiesterase. Nitrosyl iron complexes [Fe(CNHS)Cl(NO)][Fe(NO)(CNHS)]Cl (I), [Fe(SC(N(CH))(NO)]Cl (II), [Fe(SC(NH))(NO)Cl×HO (III), and [Fe(SC(NH))(NO)]SO×HO (IV) in a concentration of 10 M completely inhibited the transporting and hydrolytic functions of Ca-ATPase. In a concentration of 10 M, they inhibited active Ca transport by 57±6, 75±8, 80±8, and 85±9% and ATP hydrolysis by 0, 40±4, 48±5, and 38±4%, respectively.