Protein-protein interactions in the systems of cytochromes P450 3A4 and 3A5

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 , includin...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry (Moscow). Supplement. Series B, Biomedical chemistry Biomedical chemistry, 2014-07, Vol.8 (3), p.231-236
Main Authors: Gnedenko, O. V., Ivanov, A. S., Yablokov, E. O., Usanov, S. A., Mukha, D. V., Sergeev, G. V., Kuzikov, A. V., Moskaleva, N. E., Bulko, T. V., Shumyantseva, V. V., Archakov, A. I.
Format: Article
Language:English
Subjects:
Bioorganic Chemistry
Catalytic polymerization
Chemistry
Chemistry and Materials Science
Cytokines
Medicinal Chemistry
Proteins
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1990-7508
1990-7516
DOI:10.1134/S1990750814030068