Design of model systems based on cytochrome P450 3A4 and riboflavin complexes for increasing the electrocatalysis efficiency

Abstract

Cytochromes P450 (CYP) are a large class of enzymes, whose active site is type b heme. The main function of cytochromes P450 is biotransformation of endogenous and exogenous compounds in the organism. The cytochrome P450 3A4 metabolizes about 50% of all modern medications; therefore, its catalytic properties present significant research interest. P450 cytochromes can be effectively investigated using electrochemical systems that consist of a solid base (electrode) and a modifier facilitating enzyme immobilization. In this case, the electron donor is an electrode substituting a natural electron donor NAD(P)H and eliminating the need to use redox-partner proteins. The electrode modifier maintains the catalytic enzyme activity and enhances the efficiency of electron transfer when noble metals and carbon materials nanoparticles are included. This work is aimed at creating more effective cytochrome P450 electrochemical systems to increase the yield of metabolites of enzymatic electrocatalytic reactions.