In this brief survey, the path of development of our knowledge of the
iron-sulfur enzyme aconitase [citrate(isocitrate)hydrolyase EC4.2.1.3.
] is traced from its discovery in 1937. Particular emphasis is on deve
lopments in the past decade, when EPR, Mossbauer and electron nuclear
double resonance spectroscopies, X-ray crystallography, and mutational
analysis were applied to the problem. More recently discovered was th
e significant amino acid sequence identity between mitochondrial aconi
tase and the iron regulatory factor or iron-responsive element binding
protein (IRE-BP). This has led to the realization that IRE-BP is an a
lternative form of cytosolic (not of mitochondrial) aconitase that is
devoid of its cubane Fe-S cluster.