@article {2500,
	title = {Total synthesis of a simple metalloprotein-desulforedoxin},
	journal = {Biochem Biophys Res Commun},
	volume = {208},
	number = {2},
	year = {1995},
	note = {<p>0006-291X (Print)0006-291X (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Mar 17},
	pages = {680-7},
	abstract = {<p>Desulforedoxin is a protein purified from cellular extracts of Desulfovibrio gigas. It is a small (7.9 kDa) dimeric protein that contains a distorted rubredoxin like center (one single iron coordinated by four cysteinyl residues). Due to the simplicity of the polypeptide chain and of the iron center, an attempt was made to chemically produce this protein. A 36 amino acid polypeptide chain was synthesized based on the known sequence of native Desulforedoxin. The iron center was then reconstituted and the biochemical and spectroscopic characteristics of this synthetic protein were investigated. The final product has an equal sequence to the protein purified from D. gigas. The synthetic and natural Dx are very similar, in terms redox potential and spectroscopic properties (UV-Visible, EPR, Mossbauer).</p>
},
	keywords = {Cysteine/chemistry, Desulfovibrio/chemistry, Electron Spin Resonance Spectroscopy, Iron-Sulfur Proteins/*chemical synthesis, Spectrophotometry, Ultraviolet, Spectrum Analysis},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=7695623 },
	author = {Tavares, P and Wunderlich, J. K. and Lloyd, S. G. and Legall, J. and Moura, J. J. and Moura, I.}
}
