Ramsay R R
Biochem J. 1982 Apr 1;203(1):327-30. doi: 10.1042/bj2030327.
Reduction of the iron-sulphur cluster of aconitase initiates a slow increase in catalytic activity. It has been proposed that activation involves a conformational change in the protein. Direct evidence for this is presented here in the demonstration that, after reduction of the cluster, the progressive increase in activity is parallelled by an increase in the fluorescence of the protein.
乌头酸酶铁硫簇的还原引发催化活性的缓慢增加。有人提出,激活涉及蛋白质的构象变化。本文提供了这方面的直接证据,证明在簇还原后,活性的逐渐增加与蛋白质荧光的增加平行。