4.2.1.3 Fe a iron-mediated dimerization mechanism for switching AcnB between its catalytic and regulatory form is proposed 666394 4.2.1.3 Fe iron restriction reproducibly causes 60% decreases in both mitochondrial and cytosolic aconitase activities in erythroid samples 702863 4.2.1.3 Fe IRP1 binds a [4Fe-4S] cluster 663546 4.2.1.3 Fe2+ - 684713 4.2.1.3 Fe2+ activates the enzyme under normal conditions and in animals with toxic hepatitis. The stimulatory effect of Fe2+ in concentrations below 1 mM is less pronounced than in animals with toxic hepatitis 664485 4.2.1.3 Fe2+ enzyme activity increases 2-4fold in presence of both Fe2+ and cysteine. 0.1-1 mM Fe2+ and 0.05-0.5 mM cysteine 650272 4.2.1.3 Fe2+ iron restriction reproducibly causes 60% decreases in both mitochondrial and cytosolic aconitase activities in erythroid samples 702863 4.2.1.3 Fe2+ mitochondrial aconitase contains iron-sulfur cluster 698948 4.2.1.3 Fe2+ required 696168 4.2.1.3 Fe2+ required, binding structure in the [4Fe-4S] cluster, mechanism of activation of the enzyme by Fe2+, overview 696168