The Ukrainian Biochemical Journal (Jun 2014)

Complexes of cobalt (II, III) with derivatives of dithiocarbamic acid – effectors of peptidases of Bacillus thuringiensis and α-L-Rhamnozidase of Eupenicillium erubescens and Cryptococcus albidus

  • L. D. Varbanets,
  • E. V. Matseliukh,
  • I. I. Seifullina,
  • N. V. Khitrich,
  • N. A. Nidialkova,
  • E. V. Gudzenko

DOI
https://doi.org/10.15407/ubj86.03.049
Journal volume & issue
Vol. 86, no. 3
pp. 49 – 60

Abstract

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The influence of cobalt (II, III) coordinative compounds with derivatives of dithiocarbamic acid on Bacillus thuringiensis IMV B-7324 peptidases with elastase and fibrinolytic activi­ty and Eupenicillium erubescens and Cryptococcus albidus α-L-rhamnosidases have been studied. Tested coordinative compounds of cobalt (II, III) on the basis of their composition and structure are presented by 6 groups: 1) tetrachlorocobaltates (II) of 3,6-di(R,R′)-iminio-1,2,4,5-tetratiane – (RR′)2Ditt[CoCl4]; 2) tetrabromocobaltates (II) of 3,6-di(R,R′)-iminio-1,2,4,5-tetratiane – (RR′)2Ditt[CoBr4]; 3) isothiocyanates of tetra((R,R′)-dithiocarbamatoisothiocyanate)cobalt (II) – [Co(RR′Ditc)4](NCS)2]; 4) dithiocarbamates of cobalt (II) – [Co(S2CNRR′)2]; 5) dithiocarbamates of cobalt (III) – [Co(S2CNRR′)3]; 6) molecular complexes of dithiocarbamates of cobalt (III) with iodine­ – [Co(S2CNRR′)3]∙2I2. These groups (1-6) are combined by the presence of the same complexing agent (cobalt) and a fragment S2CNRR′ in their mole­cules. Investigated complexes differ by a charge of intrinsic coordination sphere: anionic (1-2), cationic (3) and neutral (4-6). The nature of substituents at nitrogen atoms varies in each group of complexes. It is stated that the studied coordination compounds render both activating and inhibiting effect on enzyme activity, depending on composition, structure, charge of complex, coordination number of complex former and also on the enzyme and strain producer. Maximum effect is achieved by activating of peptidases B. thuringiensis IMV B-7324 with elastase and fibrinolytic activity. So, in order to improve the catalytic properties of peptidase 1, depending on the type of exhibited activity, it is possible to recommend the following compounds: for elastase – coordinately nonsaturated complexes of cobalt (II) (1-4) containing­ short aliphatic or alicyclic substituents at atoms of nitrogen and increasing activity by 17-100% at an average; for fibrinolytic – neutral dithio­carbamates of cobalt (II, III) (4-5) (by 29-199%). For increasing the fibrinolytic activity of peptidase it is better to use dibenzyl- or ethylphenyldithiocarbamates of cobalt (III), which increase activity by 15-40% at an average. The same complexes, and also compound {(CH2)6}2Ditt[CoCl4] make an activating impact on α-L-rhamnosidase C. albidus (by 10-20%).

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