Specificity of Isatin Interaction with Cytochromes P450

Specificity of Isatin Interaction with Cytochromes P450 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 study, 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 systems: five isoforms of cytochromes P450, two isoforms of cytochrome b 5, cytochrome P450 reductase, adrenodoxin, adrenodoxin reductase and ferrochelatase. The study has shown high affinity specific binding of isatin only to cytochromes P450 (the equilibrium dissociation constant (K d) is about 10–8 M). http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry Springer Journals

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Publisher
Springer Journals
Copyright
Copyright © 2018 by Pleiades Publishing, Ltd.
Subject
Chemistry; Bioorganic Chemistry; Medicinal Chemistry
ISSN
1990-7508
eISSN
1990-7516
D.O.I.
10.1134/S1990750818020026
Publisher site
See Article on Publisher Site

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 study, 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 systems: five isoforms of cytochromes P450, two isoforms of cytochrome b 5, cytochrome P450 reductase, adrenodoxin, adrenodoxin reductase and ferrochelatase. The study has shown high affinity specific binding of isatin only to cytochromes P450 (the equilibrium dissociation constant (K d) is about 10–8 M).

Journal

Biochemistry (Moscow) Supplement Series B: Biomedical ChemistrySpringer Journals

Published: May 30, 2018

References

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