Structure and Function of Cytochrome with Cardiolipin: Enzymatic Activity of the Complex and Free-Radicals Processes

Abstract

The points of enzymatic activity, quantum yields, structure, and functions of luminol chemiluminescence activated by physical activators coumarinomics \({{C}_{{314}}}\) and \({{C}_{{525}}}\) under the action of \(CytC-CL~\)complex in aqueous medium and in a nonpolar environment have been modelled. It is shown that the enzymatic activity points and quantum yields are significantly higher in the presence of the physical activator coumarin \({{C}_{{525}}}\) than in the case of its own non-activated luminescence and in the case of the physical activator \({{C}_{{314}}}\). The enzymatic activity depends not only on the concentration of cytochrome C but also on the percentage ratio between its native and partially denatured forms. The release of the \(CytC-CL~\) complex into the cytoplasm leads to activation of membrane lipid peroxidation processes and a cascade of enzymatic reactions leading to apoptosis. Parameters investigated by kinetics of activated chemiluminescence, based on the data of cancer cells, confirm the properties to resist apoptosis and mutations, i.e. the reason for the appearance of different kinds of metastasis. The results of modelling are applicable to the analysis of natural apoptogens, which are the basis for the creation of drugs and lead to increased resistance of the organism to the effects of various factors.