Iron is important to many biological functions, such as oxygen binding in hemoglobin and serving as a cofactor in several different proteins. However, it is highly reactive, and if not properly regulated, will oxidize, creating oxygen radicals that can lead to cell damage, cell death and several long-term inflammatory conditions.<br/>Our research focuses on how the labile iron pool (LIP) is regulated. Specifically, how glutathione (GSH) stabilizes Fe(II) by chelating it, preventing it from oxidizing and reducing it if it does oxidize. We also researched how GSH improves iron loading into an iron storage protein called ferritin via an alternant mechanism. Additionally, we studied how other molecules interacted with glutathione and ferritin.<br/>To measure GS:Fe(II) stability and ferritin iron loading, we tracked Fe(II) depletion using bipyridine – a molecule that binds exclusively to Fe(II) and then absorbs light at 520nm. We measured absorbance in a spectrophotometer.<br/>We present an improved ferritin iron loading model. We also provide a novel ferritin iron loading detection method, and evidence that GSH protects Fe(II) against oxidation.

Iron regulation with glutathione and ferritin in the labile iron pool

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