Abstract
Molecular interactions between protein partners of the monooxygenase system involved in drug biotransformation (cytochromes P450 3A4, 3A5 and cytochrome b 5) have been investigated. Human cytochromes P450 3A4 and 3A5 (CYP3A4 and CYP3A5) form complexes with various forms of cytochrome b 5, including microsomal (b 5 mc) and mitochondrial (b 5 om) forms of this protein, as well as two chimeric constructs (b 5(om-mc),(b 5(mc-om). Interestingly, significant differences were observed only during interactions with b 5 om. Electroanalytical characteristics of electrodes with immobilized hemoproteins have been determined for CYP3A4, CYP3A5, b 5 mc, b 5 om, b 5 mc(om-mc), and b 5 mc(mc-om). The electrochemical analysis revealed that these proteins are characterized by close reduction potentials ranged from −0.435 V to −0.350 V (vs. Ag/AgCl). Cytochrome b 5 mc stimulated the electrocatalytic activity of CYP3A4.
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