Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1392776 | Chemistry & Biology | 2008 | 7 Pages |
Abstract
SummaryThe addition of a hexahistidine tag to the N terminus of the hepatitis B capsid protein gives rise to a self-assembled particle with 80 sites of high local density of histidine side chains. Iron protoporphyrin IX has been found to bind tightly at each of these sites, making a polyvalent system of well-defined spacing between metalloporphyrin complexes. The spectroscopic and redox properties of the resulting particle are consistent with the presence of 80 site-isolated bis(histidine)-bound heme centers, comprising a polyvalent b-type cytochrome mimic.
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Authors
Duane E. Prasuhn Jr., Jane Kuzelka, Erica Strable, Andrew K. Udit, So-Hye Cho, Gabriel C. Lander, Joel D. Quispe, James R. Diers, David F. Bocian, Clint Potter, Bridget Carragher, M.G. Finn,