Study specificity of isatin interactions with P450 cytochromes


1. Institute of Biomedical Chemistry, Moscow, Russia
2. Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, Belarus
Type: Experimental study
DOI: 10.18097/PBMC20186401061      PubMed Id: 29460836
Year: 2018 vol: 64  issue:1  pages: 61-65
Abstract: 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).
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Reference: 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., Study specificity of isatin interactions with P450 cytochromes, Biomeditsinskaya khimiya, 2018, vol: 64(1), 61-65.
This paper is also available as the English translation:10.1134/S1990750818020026
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