Evidence that the activation of aconitase involves a conformation change.
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.
D000154:Aconitate Hydratase / Q000378:metabolism*; D004227:Dithionite / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence
D004227:Dithionite; D000154:Aconitate Hydratase