FREE RADICALS. FEATURES OF CHEMILUMINESCENT ACTIVITY OF CYTOCHROME C CATALYST IN COMPLEX WITH CARDIOLIPIN

Abstract

Using the luminol chemiluminescence method for the lipid-membrane environment, which is condensed. Both lipid peroxidation processes, points of enzymatic activity, quantum yields, structure, and functions of the natural dye-activated fluorescent probe coumarin C-334 chemiluminescence under the action of a heterogeneous catalyst complex of cytochrome C with cardiolipin in aqueous medium and in a nonpolar environment were analyzed , and processes of lipid peroxidation, points of enzymatic activity, quantum yields, structure, functions of chemiluminescence activated by natural dye fluorescent probe coumarin C-525 under the action of heterogeneous catalyst of cytochrome C complex with cardiolipin in aqueous medium and in nonpolar environment. It is shown that: 1) the enzymatic activity points and quantum yields were significantly higher in the presence of the physical activator fluorescent probe natural dye coumarin C-525 than in the case of its own non-activated luminescence or in the case of the natural dye physical activator fluorescent probe coumarin C-334; 2) an important indicator was that the enzymatic activity depends not only on the concentration of cytochrome C in the heterogeneous catalyst of the complex of cytochrome C with cardiolipin, but also on the quantitative ratio determined by a directly proportional relationship in percent between its native form and partially denatured forms.