肺炎克雷伯菌的固氮酶。硫氰酸酶催化使铁蛋白的无活性二铁物种恢复活性。
Nitrogenase of Klebsiella pneumoniae. Rhodanese-catalysed restoration of activity of the inactive 2Fe species of the Fe protein.
作者信息
Pagani S, Eldridge M, Eady R R
机构信息
A.F.R.C. Unit of Nitrogen Fixation, University of Sussex, Brighton, U.K.
出版信息
Biochem J. 1987 Jun 1;244(2):485-8. doi: 10.1042/bj2440485.
Abstract
The inactive 2Fe species of the Fe protein of the nitrogenase of Klebsiella pneumoniae was generated by treating oxidized Fe protein (Kp2) with MgATP and chelator. Incubation of the 2Fe species of Kp2 with the sulphurtransferase rhodanese in the presence of thiosulphate, ferric citrate and reduced lipoate reproducibly restored activity. The extent of restoration of activity depended on the molar ratio of 2Fe Kp2 to rhodanese and was time-dependent. Re-activation did not occur in the reaction mixture lacking rhodanese.
摘要
通过用MgATP和螯合剂处理氧化型铁蛋白（Kp2），生成了肺炎克雷伯菌固氮酶铁蛋白的无活性二铁物种。在硫代硫酸盐、柠檬酸铁和还原型硫辛酸存在的情况下，将Kp2的二铁物种与硫转移酶硫氰酸酶一起孵育，可重复性地恢复活性。活性恢复的程度取决于二铁Kp2与硫氰酸酶的摩尔比，并且是时间依赖性的。在缺乏硫氰酸酶的反应混合物中不会发生再激活。
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