The [CuLBr2] complexes, where L is RRN–C(=S)–S–NHC6H11 and RR = (C2H5)2, (CH2)5, or (CH2)2O(CH2)2, have been synthesized by reacting equimolar amounts of CuBr2 in methanol and L in diethyl ether. The compounds have been studied by elemental analysis, IR spectroscopy, EPR, X-ray absorption spectroscopy, conductometry, magnetochemistry, and thermal analysis. According to IR spectroscopy data, the ligands in the complexes are bidentately coordinated to Cu(II) through the thione sulfur sulfenamide and nitrogen atoms. Exact structural parameters of the nearest environment of Cu(II) have been determined from analysis of Cu and Br K-edge EXAFS spectra. The Cu–N, Cu–S, and Cu–Br bond lengths are within 2.06–2.08, 2.24–2.49, and 2.33–2.38 Å, respectively. The EPR spectra of the complexes in a DMF solution at 293 K are described by the isotropic spin Hamiltonian with spin S = 1/2, including hyperfine coupling to the nuclear spin of the central copper atom and additional hyperfine coupling to the nuclear spins of two equivalent bromine atoms and one nitrogen atom.

Complexes ZnX2 (X = Cl, Br, I, NCS) with 1,4-piperazine-bis-carbothiosulfendiethylamide (L) of composition [Zn2(L) X4] are synthesized and characterized by methods of elementary analysis, IR-spectroscopy, thermogravimetry. It is established, that in obtained compounds ligand is coordinated to metal through the thionic sulfur atom and sulfenamide nitrogen atom with formation of two space-divided five-member metal cycles

Chloride, bromide and isothiocyanate complexes of cobalt(II) with N-substituted thiocarbamoyl-N?-pentamethylenesulfenamides (1)–(12), and also complexes of cobalt(II, Ш) with derivatives of morpholine-4-carbodithioic acid (13)–(18) have been used as modificators of enzymes of hydrolytic action — Bacillus thurin-giensis ІМВ В-7324 peptidases, Bacillus subtilis 147 and Aspergillus flavus var. oryzae 80428 amylases, Eupenicillium erubescens 248 and Cryptococcus albidus 1001 rhamnosidases. It was shown that cobalt (II, Ш) compounds influence differently on the activity of enzymes tested, exerted both inhibitory and stimulatory action. It gives a possibility to expect that manifestation of activity by complex molecule depends on ligand and anion presence — Cl–, Br– or NCS–. The high activating action of cobalt(II) complexes with N-substituted thiocarbamoyl-N?-pentamethylenesulphenamides (1)–(12) on elastase and fibrinolytic activity of peptidases compared to tris(4-morpholinecarbodithioato)cobalt(ІІІ) (14) and products of its interaction with halogens (15)–(17), causes inhibitory effect that is probably due to presence of a weekly S–N link, which is easy subjected to homolytic breaking. The studies of influences of cobalt(II) complexes on activity of C. аlbidus and E. еrubescens ?-Lrhamnosidases showed, that majority of compounds inhibits of its activity, at that the most inhibitory effect exerts to C. аlbidus enzyme.To sum up, it is possible to state that character of influence of cobalt(II) complexes with N-substituted thiocarbamoyl-N?-pentamethylenesulphenamides, and also cobalt(II, Ш) complexes with derivatives of morpholine-4-carbodithioic acid varies depending on both strain producer and enzyme tested. The difference in complex effects on enzymes tested are due to peculiarities of building and functional groups of their active centers, which are also responsible for binding with modificators.

On the base of the kinetic and activation parameters of the hydrogen peroxide decomposition in the presence of chelates of CoX2 salts (X = Cl, Br, I, NCS) with N,N,N′,N′-tetrasubstituted thiocarbamoylsulfenamides containing exocyclic (out-of-chelate) fragments of dimethylamine (I), piperidine (II), and piperazine (III) the nature of acido-ligands influence on catalase activity of complexes I–III was revealed, depending on the structure and composition of the chelating ligand. Mononuclear complexes I(Br) and II(Br) can transform into 10-membered binuclear macrochelate intermediates.

Chloride, bromide and isothiocyanate complexes of cobalt(II) with N-substituted thiocar bamoyl-N ′-pentamethylenesulfenamides (1)–(12), and also complexes of cobalt(II, Ш) with derivatives of morpholine-4-carbodithioic acid (13)–(18) have been used as modificators of enzymes of hydrolytic action — Bacillus thuringiensis ІМВ В-7324 peptidases, Bacillus subtilis 147 and Aspergillus flavus var. oryzae 80428 amylases, Eupenicillium erubescens 248 and Cryptococcus albidus 1001 rhamnosidases. It was shown that cobalt (II, Ш) compounds influence differently on the activity of enzymes tested, exerted both inhibitory and stimulatory action. It gives a possibility to expect that manifestation of activity by complex molecule depends on ligand and anion presence — Cl –, Br – or NCS –. The high activating action of cobalt(II) complexes with N-substituted thiocarbamoyl-N′pentamethylenesulphenamides (1)–(12) on elastase and fibrinolytic activity of peptidases compared to tris(4-morpholinecarbodithioato)cobalt(ІІІ) (14) and products of its interaction with halogens (15)–(17), causes inhibitory effect that is probably due to presence of a weekly S–N link, which is easy subjected to homolytic breaking. The studies of influences of cobalt(II) complexes on activity of C. аlbidus and E. еrubescens α-Lrhamnosidases showed, that majority of com pounds inhibits of its activity, at that the most inhibitory effect exerts to C. аlbidus enzyme. To sum up, it is possible to state that character of influence of cobalt(II) complexes with N-substituted thio carbamoyl-N′-pentamethylenesul phenamides, and also cobalt(II, Ш) complexes with derivatives of morpholine-4-carbodithioic acid varies depending on both strain-producer and enzyme tested. The difference in complex effects on enzymes tested are due to peculiarities of building and functional groups of their active centers, which are also responsible for binding with modificators.