Applied Biochemistry and Microbiology

, Volume 54, Issue 4, pp 370–374 | Cite as

Purification and Investigation of Physicochemical and Regulatory Properties of Homogeneous L-Lactate: Cytochrom c Oxidoreductase Obtained from the Nonsulfur Purple Bacterium Rhodovulum steppense

  • A. T. EprintsevEmail author
  • V. M. Larchenkov
  • N. R. Komarova
  • E. V. Kovaleva
  • A. V. Mitkevich
  • M. I. Falaleeva
  • E. I. Kompantseva


L-Lactate: cytochrome c oxidoreductase activity was detected in cells of strain A-20s of the nonsulfur haloalkalophilic purple bacterium Rhodovulum steppense. An electrophoretically homogeneous preparation of the enzyme was obtained by purification. The enzyme had a specific activity of 4.75 U/mg protein, a 81.9-fold purification degree, and a 2.2% yield. The kinetic and physicochemical characteristics were determined. The value of the Michaelis constant with lactate was 15 μM. The temperature optimum for the studied enzyme was 31°C; optimum of pH was 8.2. It was found that the enzyme was a homodimer with a molecular weight of ~140 kDa; the mass of individual subunit was 68 kDa.


L-lactate: cytochrome c oxidoreductase haloalkalophilic purple bacteria ion exchange chromatography gel chromatography subunit structure electrophoresis the Michaelis constant Rhodovulum steppense 


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Copyright information

© Pleiades Publishing, Inc. 2018

Authors and Affiliations

  • A. T. Eprintsev
    • 1
    Email author
  • V. M. Larchenkov
    • 1
  • N. R. Komarova
    • 1
  • E. V. Kovaleva
    • 1
  • A. V. Mitkevich
    • 1
  • M. I. Falaleeva
    • 1
  • E. I. Kompantseva
    • 2
  1. 1.Voronezh State UniversityVoronezhRussia
  2. 2.Winogradsky Institute of Microbiology, Biotechnology Research CenterRussian Academy of SciencesMoscowRussia

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