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Polyvalent display of heme on hepatitis B virus capsid protein through coordination to hexahistidine tags.


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.

SUBMITTER: Prasuhn DE 

PROVIDER: S-EPMC2715361 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature

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Polyvalent display of heme on hepatitis B virus capsid protein through coordination to hexahistidine tags.

Prasuhn Duane E DE   Kuzelka Jane J   Strable Erica E   Udit Andrew K AK   Cho So-Hye SH   Lander Gabriel C GC   Quispe Joel D JD   Diers James R JR   Bocian David F DF   Potter Clint C   Carragher Bridget B   Finn M G MG  

Chemistry & biology 20080501 5


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 c  ...[more]

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