Aconitase is an iron-sulfur protein containing a [Fe4S4]2+ cluster that catalyzes the stereo-specific isomerization of citrate to isocitrate via cis-aconitate. Exposure of aconitase to oxidants renders the enzyme inactive and loss of aconitase activity in cells or in biological samples treated with pro-oxidants has been interpreted as a measure of oxidative damage. Cayman's Fluorometric Aconitase Activity Assay provides a fluorescence-based method for detecting aconitase activity from tissue homogenates or cell lysates. In this assay, citrate is isomerized by aconitase into isocitric, which is then converted to (alpha)-ketoglutarate in a reaction catalyzed by isocitrate dehydrogenase. These reactions are monitored by measuring the formation of NADPH in a reaction with a substrate that yields a highly fluorescent product. Under appropriate conditions, the rate of NADPH production is proportional to aconitase activity.