Article
Polyvalent Display of Heme on Hepatitis B Virus Capsid Protein through Coordination to Hexahistidine Tags
Chemistry & Biology
(2008)
Abstract
The 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.
Disciplines
Publication Date
May 19, 2008
Citation Information
Duane E Prasuhn, Jane Kuzelka, Erica Strable, Andrew K Udit, et al.. "Polyvalent Display of Heme on Hepatitis B Virus Capsid Protein through Coordination to Hexahistidine Tags" Chemistry & Biology Vol. 15 Iss. 5 (2008) Available at: http://works.bepress.com/udit/4/