Kakutani T, Watanabe H, Arima K, Beppu T
J Biochem. 1981 Feb;89(2):453-61. doi: 10.1093/oxfordjournals.jbchem.a133220.
A copper-containing nitrite reductase was purified and crystallized from a potent denitrifying bacterium, Alcaligenes faecalis strain S-6. The enzyme was composed of 4 subunits with a molecular weight of about 30,000, each containing 1 atom of Cu2+. Nitric oxide was identified as a main reduction product from nitrite in the enzyme-catalyzed reaction. The enzyme activity was inhibited strongly by KCN but only slightly by sulfhydryl reagents such as p-chloromercuribenzoate and N-ethylmaleimide.
从高效反硝化细菌粪产碱菌S-6菌株中纯化并结晶出一种含铜亚硝酸还原酶。该酶由4个亚基组成，分子量约为30,000，每个亚基含有1个Cu2+原子。在酶催化反应中，一氧化氮被鉴定为亚硝酸的主要还原产物。该酶活性受到KCN的强烈抑制，但仅受到对氯汞苯甲酸和N-乙基马来酰亚胺等巯基试剂的轻微抑制。
