Ershov P V, Mezentsev Yu V, Yablokov E O, Kalushskiy L A, Florinskaya A V, Svirid A V, Gilep A A, Usanov S A, Medvedev A E, Ivanov A S
Institute of Biomedical Chemistry, Moscow, Russia.
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, Belarus.
Biomed Khim. 2018 Jan;64(1):61-65. doi: 10.18097/PBMC20186401061.
Cytochrome P450-dependent monooxygenase systems exist basically in all living organisms, where they perform various important functions. The coordinated functioning of these systems involves many proteins participating in different protein-protein interactions (PPI). Previously, we have found that the endogenous non-peptide bioregulator isatin (indoledione-2,3), synthesized from indole by means of certain cytochromes P450 (e.g. P450 2E1, P450 2C19, P450 2A6) regulates affinity of some PPI. In this work, an attempt has been undertaken to register a direct interaction of isatin with a set of different proteins related to the functioning of cytochrome P450-dependent monooxygenase: five isoforms of cytochromes P450, two isoforms of cytochrome b5, cytochrome P450 reductase, adrenodoxin, adrenodoxin reductase and ferrochelatase. The study has shown that isatin binds specifically only to cytochromes P450 with high affinity (the equilibrium dissociation constant (Kd) is about 10-8 M).
