Purification and Investigation of Physicochemical and Regulatory Properties of Homogeneous L-Lactate: Cytochrom <Emphasis Type="Italic">c</Emphasis> Oxidoreductase Obtained from the Nonsulfur Purple Bacterium <Emphasis Type="Italic">Rhodovulum steppense</Emphasis> |
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Authors: | A T Eprintsev V M Larchenkov N R Komarova E V Kovaleva A V Mitkevich M I Falaleeva E I Kompantseva |
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Institution: | 1.Voronezh State University,Voronezh,Russia;2.Winogradsky Institute of Microbiology, Biotechnology Research Center,Russian Academy of Sciences,Moscow,Russia |
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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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