| Literature DB >> 15134929 |
S A Bursakov1, O Yu Gavel, G Di Rocco, J Lampreia, J Calvete, A S Pereira, J J G Moura, I Moura.
Abstract
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.Entities:
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Year: 2004 PMID： 15134929 DOI： 10.1016/j.jinorgbio.2003.12.002
Source DB: PubMed Journal: J Inorg Biochem ISSN： 0162-0134 Impact factor: 4.155