| The proposed structure for E. coli bacterioferritn is closely related
to the human H-chain ferritin. To see more about the overal structure of
bacterioferritns and it's relation to ferritins click here. The quaternary structure of bacterioferritins shows a rough spherical shape allowing for many inter subunit interactions. These inter subunit interactions help to generate fourfold and threefold channels. Click here to learn more about these channels. The proposed structure of bacterioferritin possesses a ferroxidase center
resposible for bringing in free iron mot associated with heme and detoxifying
it. Click here The bacterioferritin model offers two steriochemically feasible sites for heme binding. Both sites possess methionine residues aligned in a position which allows for bis-methionine axial ligation. Site I is fully contained within a subunit, whereas Site II is an inter subunit site lying at a twofold symmetry of axis. To see how Site I heme binding occurs click here.
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Caleb W. Dorsey
Student of
Scott
Hartsel
Department of Chemistry
(715) 836-4746
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