Abstract
In the present study, the effects of endogenous non-peptide bioregulator isatin (indole-2,3-dione) cytochrome P450 isoenzymes 3A5, 3A4, 2C19, 2E1, and 5A1 were investigated for the first time by means of electrochemical methods. Absorption spectroscopy and electrochemical methods have shown that isatin does not interact with heme as the active center of cytochrome P450 isoenzymes. Isatin has no significant effect on the electrocatalysis of cytochrome P450 3A4 (CYP3A4) in the presence of testosterone chosen as the substrate. Direct electrochemistry of thromboxane synthase (CYP5A1 or TBXAS1) has been investigated using protein film voltammetry. Reversible electrochemical signals of CYP5A1 were observed with midpoint potential of − 0.294 ± 0.012 V (vs Ag/AgCl). The results obtained indicate the existence of the binding sites for isatin on the protein surface of the investigated cytochromes P450, which differ from the active substrate-binding center. For CYP3A4 Arg375, Arg105, and Arg440; for CYP3A5 Arg375 and Arg105; and for CYP2C19 Arg433 were revealed as conserved “hot” amino acid residues involved in the binding of isatin while aligning CYP’s sequences.
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