Isolation, purification and characterization of hemerythrin from Methylococcus capsulatus (Bath)
Resource
Journal of Inorganic Biochemistry 102 (8): 1607-1614
Journal
Journal of Inorganic Biochemistry
Pages
1607-1614
Date Issued
2008
Date
2008
Author(s)
Kao, Wei-Chun
Wang, Vincent C.-C.
Huang, Yi-Che
Yu, Steve S.-F.
Chang, Ta-Chau
Chan, Sunney I.
Abstract
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.
Type
journal article
File(s)![Thumbnail Image]()
Loading...
Name
17.pdf
Size
574.39 KB
Format
Adobe PDF
Checksum
(MD5):15410fed8ea2fb3423a70de73d91c467