Preston G G, Ludden P W
Biochem J. 1982 Sep 1;205(3):489-94. doi: 10.1042/bj2050489.
The subunit composition of the Fe protein of nitrogenase from Rhodospirillum rubrum during activation and inactivation was investigated. It was found that the upper subunit (on gel electrophoresis) of the two-subunit Fe protein was converted into the lower subunit during activation in vitro. When the Fe protein was inactivated in vivo by the addition of NH4Cl and alpha-oxoglutarate to the cells, a phosphate-labelled upper band appeared. During activation in vitro by the activating enzyme, some of the phosphate of the upper band remained with the protein and appeared in the lower band. Activations in vitro were performed on inactive Fe protein obtained from cells grown with glutamate as the nitrogen source. Both native and oxygen-denatured Fe protein exhibited the loss of upper band during treatment with activating enzyme.
研究了深红红螺菌固氮酶铁蛋白在激活和失活过程中的亚基组成。发现在体外激活过程中，两亚基铁蛋白的上亚基（在凝胶电泳中）转化为下亚基。当通过向细胞中添加氯化铵和α-酮戊二酸使铁蛋白在体内失活时，出现了一条磷酸化标记的上带。在体外由激活酶激活过程中，上带的一些磷酸基团仍与蛋白质结合并出现在下带中。对以谷氨酸作为氮源生长的细胞中获得的无活性铁蛋白进行了体外激活。天然和氧变性的铁蛋白在用激活酶处理过程中均表现出上带的消失。
