Abstract
The process of biomimetic monooxidation of ethylene into ethyl alcohol and acetaldehyde by hydrogen peroxide on the per-FTPhPFe3+OH/Al2O3 bioimitator, which showed high activity and unique resistance to the action of high-active intermediate reaction products was investigated. As a result of studying the kinetic regularities of the selective biomimetic oxidation of ethylene by hydrogen peroxide, a coherent-synchronized nature of the reaction was observed, consisting of two reactions: 1) primary (catalase) and 2) secondary (monooxygenase and peroxidase) reactions. A new approach to the kinetic modeling based on the determinant equation and coherence correlation of catalase-monooxygenase and catalase-peroxidase reactions coherently synchronized with each other was developed. The kinetic model of the process was developed on the basis of the determinant equation, which allows assessing the coherent nature of synchronously flowing reactions both qualitatively and quantitatively. Effective rate constants of catalase, monooxygenase and peroxidase reactions were determined based on this model as well as their effective activation energies were calculated.