Abstract
Nitrate reductase from the haloalkalophilic denitrifying bacterium Halomonas sp. Strain AGJ 1-3 was isolated and purified to homogeneity. The isolated enzyme belongs to a novel family of molybdenum-free nitrate reductases. It presents as a 130–140 kD monomeric protein with specific activity of 250 µmol/min per mg protein. The enzyme reduces not only nitrate, but also other anions, thus showing polyoxoanion reductase activity. Enzyme activity was maximal at pH 7.0 and 70–80°C.
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Translated from Biokhimiya, Vol. 70, No. 7, 2005, pp. 968–973.
Original Russian Text Copyright © 2005 by Antipov, Morozkina, Sorokin, Golubeva, Zvyagilskaya, L’vov.
Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM04-165, February 13, 2005.
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Antipov, A.N., Morozkina, E.V., Sorokin, D.Y. et al. Characterization of Molybdenum-Free Nitrate Reductase from Haloalkalophilic Bacterium Halomonas sp. Strain AGJ 1-3. Biochemistry (Moscow) 70, 799–803 (2005). https://doi.org/10.1007/s10541-005-0186-0
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DOI: https://doi.org/10.1007/s10541-005-0186-0