Gawron O, Waheed A, Glaid A J, Jaklitsch A
Biochem J. 1974 Jun;139(3):709-14. doi: 10.1042/bj1390709.
Aconitase activated with Fe(2+), cysteine and ascorbate incorporates 1 g-atom of Fe(2+)/mol. Loss of this Fe(2+) by transfer to ferrozine, a Fe(2+) chelator, results in loss of activity. Ascorbate increases the rate of transfer of the essential Fe(2+) whereas citrate retards the rate of transfer. Transfer of Fe(2+) from inactive aconitase, 2 g-atoms of Fe/mol, can be accomplished in the presence of urea and ascorbate. The correlation of activity with the presence of an added g-atom of Fe(2+)/mol leads to the conclusion that active aconitase has only one active site per mol.
用Fe(2+)、半胱氨酸和抗坏血酸激活的乌头酸酶每摩尔结合1克原子的Fe(2+)。通过将这种Fe(2+)转移至Fe(2+)螯合剂亚铁嗪会导致活性丧失。抗坏血酸增加了必需Fe(2+)的转移速率,而柠檬酸盐则减缓了转移速率。在尿素和抗坏血酸存在的情况下,可以实现从无活性的乌头酸酶(每摩尔2克原子的Fe)转移Fe(2+)。活性与每摩尔添加1克原子Fe(2+)的相关性得出结论:活性乌头酸酶每摩尔只有一个活性位点。