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

Chem Biol. 2008 May;15(5):513-9. doi: 10.1016/j.chembiol.2008.03.018.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Capsid / chemistry
  • Capsid / metabolism*
  • Chromatography, Gel
  • Cryoelectron Microscopy
  • DNA Primers
  • Heme / metabolism*
  • Hepatitis B virus / metabolism*
  • Histidine / chemistry
  • Histidine / metabolism*
  • Oligopeptides / chemistry
  • Oligopeptides / metabolism*
  • Spectrum Analysis, Raman


  • DNA Primers
  • His-His-His-His-His-His
  • Oligopeptides
  • Heme
  • Histidine