@article {581,
	title = {Isolation, purification and characterization of hemerythrin from Methylococcus capsulatus (Bath)},
	journal = {Journal of Inorganic Biochemistry},
	volume = {102},
	number = {8},
	year = {2008},
	note = {<p>331KVTimes Cited:13Cited References Count:23</p>
},
	month = {Aug},
	pages = {1607-1614},
	abstract = {<p>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. (c) 2008 Elsevier Inc. All rights reserved.</p>
},
	keywords = {bacterial chemotaxis protein, domain, electron paramagnetic resonance, hemerythrin, methane monooxygenase, methylococcus capsulatus (bath), multiple sequence alignment, particulate methane monooxygenase, protein purification, resonance raman spectroscopy},
	isbn = {0162-0134},
	url = {<Go to ISI>://WOS:000258012000007},
	author = {Kao, W. C. and Wang, V. C. C. and Huang, Y. C. and Yu, S. S. F. and Chang, T. C. and Chan, S. I.}
}
