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 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.
Antipov
A N
AN
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia. a_antipov@hotbox.ru
Morozkina
E V
EV
Sorokin
D Yu
DY
Golubeva
L I
LI
Zvyagilskaya
R A
RA
L'vov
N P
NP
D000838:Anions / Q000737:chemistry / Q000378:metabolism; D020632:Halomonas / Q000145:classification / Q000201:enzymology* / Q000254:growth & development; D006863:Hydrogen-Ion Concentration; D009566:Nitrates / Q000737:chemistry / Q000378:metabolism; D009572:Nitrite Reductases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D013696:Temperature
D000838:Anions; D009566:Nitrates; D009572:Nitrite Reductases