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

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Abstract

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.

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Authors and Affiliations

  1. Voronezh State University, Voronezh, 394006, Russia

    A. T. Eprintsev, V. M. Larchenkov, N. R. Komarova, E. V. Kovaleva, A. V. Mitkevich & M. I. Falaleeva

  2. Winogradsky Institute of Microbiology, Biotechnology Research Center, Russian Academy of Sciences, Moscow, 119071, Russia

    E. I. Kompantseva

Authors
  1. A. T. Eprintsev
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  2. V. M. Larchenkov
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  3. N. R. Komarova
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  4. E. V. Kovaleva
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  5. A. V. Mitkevich
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  6. M. I. Falaleeva
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  7. E. I. Kompantseva
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Correspondence to A. T. Eprintsev.

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Original Russian Text © A.T. Eprintsev, V.M. Larchenkov, N.R. Komarova, E.V. Kovaleva, A.V. Mitkevich, M.I. Falaleeva, E.I. Kompantseva, 2018, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2018, Vol. 54, No. 4.

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Eprintsev, A.T., Larchenkov, V.M., Komarova, N.R. et al. Purification and Investigation of Physicochemical and Regulatory Properties of Homogeneous L-Lactate: Cytochrom c Oxidoreductase Obtained from the Nonsulfur Purple Bacterium Rhodovulum steppense. Appl Biochem Microbiol 54, 370–374 (2018). https://doi.org/10.1134/S0003683818040063

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  • DOI: https://doi.org/10.1134/S0003683818040063

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