Biochemistry (Moscow)

, Volume 80, Issue 3, pp 366–373 | Cite as

Taurine modulates catalytic activity of cytochrome P450 3A4

  • V. V. ShumyantsevaEmail author
  • A. A. Makhova
  • T. V. Bulko
  • R. Bernhardt
  • A. V. Kuzikov
  • E. V. Shich
  • V. G. Kukes
  • A. I. Archakov


The influence of the biologically active compound taurine on the stability and catalytic properties of the hemoprotein cytochrome P450 3A4 has been investigated. The catalytic properties were analyzed by electrochemical methods (cyclic and square-wave voltammetry) using cytochrome P450 3A4 immobilized on the electrode. Taurine at concentrations in the range 10–70 μM stimulated the electrochemical reduction of cytochrome P450 3A4, and the reduction was the highest (115 ± 3%) in the presence of 50 μM taurine. Taurine pronouncedly attenuated the itraconazol-caused inhibition of the P450 isoenzyme P450 3A4. Taurine protected cytochrome P450 3A4 due to stabilizing it during electrolysis at controlled voltage in the presence of erythromycin as a substrate. This protection was manifested by an increase in the amount of the “residual” reduced form of the hemoprotein (52 ± 5 and 71 ± 8%, respectively).

Key words

cytochrome P450 antioxidants drug metabolism bioelectrochemistry taurine 



didodecyldimethylammonium bromide


reactive oxygen species


square-wave voltammetry


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Copyright information

© Pleiades Publishing, Ltd. 2015

Authors and Affiliations

  • V. V. Shumyantseva
    • 1
    Email author
  • A. A. Makhova
    • 2
  • T. V. Bulko
    • 1
  • R. Bernhardt
    • 3
  • A. V. Kuzikov
    • 1
  • E. V. Shich
    • 2
  • V. G. Kukes
    • 2
  • A. I. Archakov
    • 1
  1. 1.Orekhovich Institute of Biomedical ChemistryMoscowRussia
  2. 2.Sechenov First Moscow State Medical UniversityMoscowRussia
  3. 3.Institute for BiochemistrySaarland UniversitySaarbruckenGermany

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