Ananiadi L I, Sergeev N S, Kil'dibekov N A, L'vov N P, Kretovich V L
Biokhimiia. 1983 Jun;48(6):932-6.
Milk xanthine oxidase possesses the nitrate reductase activity at pH 5.2; the pH optimum of the xanthine oxidase activity for the enzyme lies at 9.6. After removal of FAD and binding of Mo and Fe with a simultaneous measurement at the pH optima of the above activities it was found that only the Mo-containing site is necessary for the nitrate reductase activity. The switch-over of the enzyme from the xanthine oxidase to the nitrate reductase activity is associated with considerable conformational changes of the enzyme molecule.
牛奶黄嘌呤氧化酶在pH 5.2时具有硝酸还原酶活性;该酶黄嘌呤氧化酶活性的最适pH值为9.6。去除黄素腺嘌呤二核苷酸(FAD)并结合钼(Mo)和铁(Fe),同时在上述活性的最适pH值下进行测量,发现仅含钼位点对于硝酸还原酶活性是必需的。酶从黄嘌呤氧化酶活性转换为硝酸还原酶活性与酶分子相当大的构象变化有关。