Antipov A N, Morozkina E V, Sorokin D Yu, Golubeva L I, Zvyagilskaya R A, L'vov N P
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia.
Biochemistry (Mosc). 2005 Jul;70(7):799-803. doi: 10.1007/s10541-005-0186-0.
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.
从嗜盐碱反硝化细菌盐单胞菌属AGJ 1-3菌株中分离并纯化出硝酸还原酶，使其达到同质状态。分离出的酶属于一个无钼硝酸还原酶的新家族。它表现为一种130 - 140 kD的单体蛋白，比活性为每毫克蛋白250微摩尔/分钟。该酶不仅能还原硝酸盐，还能还原其他阴离子，因此具有多聚氧阴离子还原酶活性。酶活性在pH 7.0和70 - 80摄氏度时达到最大值。
