Polyvalent display of heme on hepatitis B virus capsid protein through coordination to hexahistidine tags |
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Authors: | Prasuhn Duane E Kuzelka Jane Strable Erica Udit Andrew K Cho So-Hye Lander Gabriel C Quispe Joel D Diers James R Bocian David F Potter Clint Carragher Bridget Finn M G |
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Institution: | Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA. |
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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. |
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