@article {2379,
	title = {Antagonists Mo and Cu in a heterometallic cluster present on a novel protein (orange protein) isolated from Desulfovibrio gigas},
	journal = {J Inorg Biochem},
	volume = {98},
	number = {5},
	year = {2004},
	note = {<p>0162-0134 (Print)0162-0134 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {May},
	pages = {833-40},
	abstract = {<p>An orange-coloured protein (ORP) isolated from Desulfovibrio gigas, a sulphate reducer, has been previously shown by extended X-ray absorption fine structure (EXAFS) to contain a novel mixed-metal sulphide cluster of the type [S(2)MoS(2)CuS(2)MoS(2)] [J. Am. Chem. Soc. 122 (2000) 8321]. We report here the purification and the biochemical/spectroscopic characterisation of this novel protein. ORP is a soluble monomeric protein (11.8 kDa). The cluster is non-covalently bound to the polypeptide chain. The presence of a MoS(4)(2-) moiety in the structure of the cofactor contributes with a quite characteristic UV-Vis spectra, exhibiting an orange colour, with intense absorption peaks at 480 and 338 nm. Pure ORP reveals an Abs(480)/Abs(338) ratio of 0.535. The gene sequence coding for ORP as well as the amino acid sequence was determined. The putative biological function of ORP is discussed.</p>
},
	keywords = {Amino Acid Sequence, Bacterial Proteins/*chemistry/genetics/isolation \& purification, Base Sequence, Cloning, Molecular, Copper/*chemistry, Desulfovibrio gigas/*chemistry/genetics, DNA, Bacterial/genetics, Metalloproteins/*chemistry/genetics/isolation \& purification, Molecular Sequence Data, Molecular Structure, Molybdenum/*chemistry, Sequence Homology, Amino Acid, Spectrum Analysis},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=15134929 },
	author = {Bursakov, S. A. and Gavel, O. Y. and Di Rocco, G. and Lampreia, J. and Calvete, J. and Pereira, A. S. and Moura, J. J. and Moura, I.}
}
