V. V. Shumyantseva, T. V. Bulko, O. V. Gnedenko, E. O. Yablokov, S. A. Usanov, A. S. Ivanov
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引用次数: 0
Abstract—
The role of partner proteins in the formation of functional complexes in cytochrome P450 systems was investigated by means of the optical biosensor technique, used to determine kinetic constants and equilibrium dissociation constants of complexes of cytochrome CYP11A1 (P450scc) with wild-type adrenodoxin (Adx WT) and mutant forms of adrenodoxin R106D and D109R. Wild-type adrenodoxin (Kd = (1.23 ± 0.09) × 10–6 M) and mutant D109R (Kd = (2.37 ± 0.09) × 10–8 M) formed complexes with cytochrome P450scc. In the case of the R106D mutant, no complex formation was detected. The possibility of participation of adrenodoxins and their mutant variants in the process of electron transfer as electron donors in mitochondrial cytochrome P450 systems, was assessed studying the electrochemical properties of these iron-sulfur proteins Adx WT and mutant forms of adrenodoxins. Adx WT, mutant forms R106D and D109R have redox potentials E1/2 significantly more negative than cytochromes P450 (–579 ± 10 mV, –590 ± 15 mV, and –528 ± 10 mV, respectively). These results suggest that Adx WT and mutant forms may be electron donors in the cytochrome P450 systems.
期刊介绍:
Biochemistry (Moscow), Supplement Series B: Biomedical Chemistry covers all major aspects of biomedical chemistry and related areas, including proteomics and molecular biology of (patho)physiological processes, biochemistry, neurochemistry, immunochemistry and clinical chemistry, bioinformatics, gene therapy, drug design and delivery, biochemical pharmacology, introduction and advertisement of new (biochemical) methods into experimental and clinical medicine. The journal also publishes review articles. All issues of the journal usually contain solicited reviews.