Adrenodoxins and their role in the cytochrome P450 systems

Shumyantseva V.V.1, Bulko T.V.2, Gnedenko O.V.2 , Yablokov E.O.2, Usanov S.A.3, Ivanov A.S.2

1. Institute of Biomedical Chemistry, Moscow, Russia; Pirogov Russian National Research Medical University, Moscow, Russia
2. Institute of Biomedical Chemistry, Moscow, Russia
3. Institute of Bioorganic Chemistry, Minsk, Belarus
Section: Experimental Study
DOI: 10.18097/PBMC20226801047      PubMed Id: 35221296
Year: 2022  Volume: 68  Issue: 1  Pages: 47-54
The role of partner proteins in the formation of functional complexes in cytochrome P450 systems was investigated by means of optical biosensor technique. 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 were determined using an optical biosensor. 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. For the R106D mutant, no complex formation was detected. To investigate the possibility of the participation of adrenodoxins and their mutant variants in the process of electron transfer as electron donors in mitochondrial cytochrome P450 systems, the electrochemical properties of these iron-sulfur proteins Adx WT and mutant forms of adrenodoxins were studied. 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.
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Keywords: adrenodoxine, mutant forms, cytochrome P450, surface plasmon resonance (SPR), electroanalysis, redox potential

Shumyantseva, V. V., Bulko, T. V., Gnedenko, O. V., Yablokov, E. O., Usanov, S. A., Ivanov, A. S. (2022). Adrenodoxins and their role in the cytochrome P450 systems. Biomeditsinskaya Khimiya, 68(1), 47-54.
This paper is also available as the English translation: 10.1134/S1990750822030106
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