An orange- coloured (ORP) protein from D.gigas, a sulphate reducer bacterium, has been previously shown by extended X-ray absorption fine structure to contain a novel mixed-metal sulphide cluster of the type of [S2MoS2CuS2MoS2]. We report here the purification and the biochemical/spectroscopic characterisation of this novel protein. The cluster is not covalently bound to the polypeptide chain. The gene sequence coding for ORP as well as the amino acid sequence was determined. The putative biologic function of ORP was discussed.
Antagonists Mo and Cu in a heterometallic cluster present on a novel protein (orange protein) isolated from Desulfovibrio gigas / S. A., Bursakov; Gavel, O. Y. u.; DI ROCCO, Giulia; J., Lampreia; J., Calvete; A. S., Pereira; J. J. G., Moura; I., Moura. - In: BIOCHEMISTRY. - ISSN 0006-2960. - ELETTRONICO. - 98:5(2004), pp. 833-840. [10.1016/j.jinorgbio.2003.12.002]
Antagonists Mo and Cu in a heterometallic cluster present on a novel protein (orange protein) isolated from Desulfovibrio gigas
DI ROCCO, Giulia;
2004
Abstract
An orange- coloured (ORP) protein from D.gigas, a sulphate reducer bacterium, has been previously shown by extended X-ray absorption fine structure to contain a novel mixed-metal sulphide cluster of the type of [S2MoS2CuS2MoS2]. We report here the purification and the biochemical/spectroscopic characterisation of this novel protein. The cluster is not covalently bound to the polypeptide chain. The gene sequence coding for ORP as well as the amino acid sequence was determined. The putative biologic function of ORP was discussed.
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