| Autor: |
Antipov, A. N., Morozkina, E. V., Sorokin, D. Yu., Golubeva, L. I., Zvyagilskaya, R. A., L'vov, N. P. |
| Předmět: |
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| Zdroj: |
Biochemistry (00062979); Jul2005, Vol. 70 Issue 7, p799-803, 5p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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