Guerrero M G, Jetschmann K, Völker W
Biochim Biophys Acta. 1977 May 12;482(1):19-26. doi: 10.1016/0005-2744(77)90349-7.
The stereospecificity of the hydrogen removal from reduced pyridine nucleotides catalyzed by nitrate reductase (NADH : nitrate oxidoreductase, EC 1.6.6.1, and NAD(P)H : nitrate oxidoreductase, EC 1.6.6.2) was investigated. A high degree of enzyme purification was required to obtain conclusive results. Improvements are described for the purification of nitrate reductase from Chlorella fusca and from spinach (Spinacea oleracea, L.) leaves. The latter enzyme is shown to contain a cytochrome. With highly purified nitrate reductase preparations from Cl. fusca, Neurospora crassa, Rhodotorula glutinis and spinach leaves the stereospecificity of the reaction was determined to be predominantly of the A-type in all cases.
研究了由硝酸还原酶(NADH:硝酸氧化还原酶,EC 1.6.6.1,以及NAD(P)H:硝酸氧化还原酶,EC 1.6.6.2)催化的从还原型吡啶核苷酸中去除氢的立体特异性。需要高度纯化的酶才能获得确凿的结果。描述了从fusca小球藻和菠菜(Spinacea oleracea,L.)叶片中纯化硝酸还原酶的改进方法。结果表明,后一种酶含有一种细胞色素。使用来自fusca小球藻、粗糙脉孢菌、粘红酵母和菠菜叶片的高度纯化的硝酸还原酶制剂,确定在所有情况下该反应的立体特异性主要为A型。