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...
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| Veröffentlicht in: | Biochemistry (Moscow). Supplement. Series B, Biomedical chemistry Biomedical chemistry, 2014-07, Vol.8 (3), p.231-236 |
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| Hauptverfasser: | , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
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| Zusammenfassung: | 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 |