Isolation, purification and characterization of hemerythrin from Methylococcus capsulatus (Bath)

J Inorg Biochem. 2008 Aug;102(8):1607-14. doi: 10.1016/j.jinorgbio.2008.02.008. Epub 2008 Mar 2.


Earlier work from our laboratory has indicated that a hemerythrin-like protein was over-produced together with the particulate methane monooxygenase (pMMO) when Methylococcus capsulatus (Bath) was grown under high copper concentrations. A homologue of hemerythrin had not previously been found in any prokaryote. To confirm its identity as a hemerythrin, we have isolated and purified this protein by ion-exchange, gel-filtration and hydrophobic interaction chromatography, and characterized it by mass spectrometry, UV-visible, CD, EPR and resonance Raman spectroscopy. On the basis of biophysical and multiple sequence alignment analysis, the protein isolated from M. capsulatus (Bath) is in accord with hemerythrins previously reported from higher organisms. Determination of the Fe content in conjunction with molecular-weight estimation and mass analysis indicates that the native hemerythrin in M. capsulatus (Bath) is a monomer with molecular mass 14.8 kDa, in contrast to hemerythrins from other eukaryotic organisms, where they typically exist as a tetramer or higher oligomers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hemerythrin / isolation & purification*
  • Iron / analysis
  • Methylococcus capsulatus / chemistry*
  • Molecular Weight
  • Oxygenases
  • Spectrum Analysis


  • Hemerythrin
  • Iron
  • Oxygenases
  • methane monooxygenase