Antagonists Mo and Cu in a heterometallic cluster present on a novel protein (orange protein) isolated from Desulfovibrio gigas

J Inorg Biochem. 2004 May;98(5):833-40. doi: 10.1016/j.jinorgbio.2003.12.002.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Base Sequence
  • Cloning, Molecular
  • Copper / chemistry*
  • DNA, Bacterial / genetics
  • Desulfovibrio gigas / chemistry*
  • Desulfovibrio gigas / genetics
  • Metalloproteins / chemistry*
  • Metalloproteins / genetics
  • Metalloproteins / isolation & purification
  • Molecular Sequence Data
  • Molecular Structure
  • Molybdenum / chemistry*
  • Sequence Homology, Amino Acid
  • Spectrum Analysis

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • Metalloproteins
  • Copper
  • Molybdenum