Oligomeric state investigation of flavocytochrome CYP102A1 using AFM with standard and supersharp probes

  • Yu. D. Ivanov
  • N. S. Bukharina
  • P. A. Frantsuzov
  • T. O. Pleshakova
  • N. V. Krohin
  • S. L. Kanashenko
  • A. I. Archakov


Atomic force microscopy with two types of probes—standard (radius of curvature R ∼ 10 nm) and supersharp (R ∼ 2 nm)—was used to determine an oligomeric state of CYP102A1. Using the standard probes CYP102A1 images were obtained in liquid, air and vacuum environments, and a CYP102A1 monomer: oligomer ratio α ≈ 1 was also determined. However, the use of standard probes did not allow to resolve structures of these oligomers. Using the supersharp probes it was possible to determine not only the monomer: oligomer ratio, but also to evaluate the dimer: trimer: tetramer ratio in vacuum. Thus, the ratio α for CYP102A1 in liquid can be determined by the standard probes in liquid, air, and vacuum, while oligomeric states of this protein can be specified by using the supersharp probes in vacuum.


atomic force microscopy cytochrome P450 CYP102A1 oligomeric state 


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Copyright information

© Pleiades Publishing, Ltd. 2012

Authors and Affiliations

  • Yu. D. Ivanov
    • 1
  • N. S. Bukharina
    • 1
  • P. A. Frantsuzov
    • 1
  • T. O. Pleshakova
    • 1
  • N. V. Krohin
    • 1
  • S. L. Kanashenko
    • 1
  • A. I. Archakov
    • 1
  1. 1.Orekhovich Institute of Biomedical Chemistry of Russian Academy of Medical SciencesMoscowRussia

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