Date of Award
Chemistry and Biochemistry
A strain of Escherichia coli was genetically modified to co-express human heme oxygenase-1 and ferritin. The E. coli were then grown with varying amounts of hemin to see if the iron released upon degradation of the hemin by heme oxygenase-1 is loaded into ferritin. Following incubation, the ferritin was purified and the amount of iron loaded into ferritin determined. It was found that ferritin purifed from E. coli expressing human heme oxygenase-1 contained more iron than E. coli that did not contain human heme oxygenase-1. It was concluded that some of the iron released upon degradation of hemin by heme oxygenase-1 can be sequestered by ferritin.
Gardner, Jonathan Mark, "The Fate of Iron Released from Heme by Hemeoxygenase-1" (2006). Undergraduate Honors Capstone Projects. 753.
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Steven D. Aust
Departmental Honors Advisor