Date of Award


Degree Type


Degree Name

Departmental Honors


Chemistry and Biochemistry


Ferritin is the iron storage protein found in humans, animals, plants, fungi and bacteria. We are interested in how iron is loaded and stored in mammalian ferritin. Ferrous iron must be oxidized to ferric iron in order to be stored in ferritin. It is generally believed that ferritin does the loading itself, dependant upon a "ferroxidase activity." Oxidation of iron can result in the production of the hydroxyl radical which can cause oxidative damage to surrounding proteins and other biomolecules. An indicator of oxidative damage to proteins is the formation of carbonyl groups. Using only the H subunit of human ferritin expressed in Escherichia coli to make H homomers, we studied the amount of oxidative damage to ferritin based on the amount of iron available for loading into ferritin. We are interested to see if the amount of oxidative damage to ferritin increases as the amount of available iron increases. The carbonyl assay has yet to yield any results so no conclusions can be made at this time. There is another carbonyl group assay that has yet to be used.

Included in

Chemistry Commons



Faculty Mentor

Steve D. Aust

Departmental Honors Advisor

Steve Scheiner