Characterization of molybdenum-free nitrate reductase from haloalkalophilic bacterium Halomonas sp. strain AGJ 1-3

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 m...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2005-07, Vol.70 (7), p.799-803
Main Authors: Antipov, A N, Morozkina, E V, Sorokin, D Yu, Golubeva, L I, Zvyagilskaya, R A, L'vov, N P
Format: Article
Language:English
Subjects:
Anions
Anions - chemistry
Anions - metabolism
Denitrification
Enzymatic activity
Enzymes
Halomonas
Halomonas - classification
Halomonas - enzymology
Halomonas - growth & development
Hydrogen-Ion Concentration
Molybdenum
Nitrates
Nitrates - chemistry
Nitrates - metabolism
Nitrite Reductases - chemistry
Nitrite Reductases - isolation & purification
Nitrite Reductases - metabolism
Temperature
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Summary: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 micromol/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 degrees C.
ISSN:0006-2979
1608-3040
0320-9725
DOI:10.1007/s10541-005-0186-0