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A
ADENYLYLSULFATE REDUCTASES FROM SULFATE-REDUCING BACTERIA, Lampreia, J., Pereira A. S., and Moura J. J. G. , Volume {243}, 525 B STREET, SUITE 1900, SAN DIEGO, CA 92101-4495, p.{241-260}, (1994) Abstract
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Antagonists Mo and Cu in a heterometallic cluster present on a novel protein (orange protein) isolated from Desulfovibrio gigas, Bursakov, S. A., Gavel O. Y., Di Rocco G., Lampreia J., Calvete J., Pereira A. S., Moura J. J. G., and Moura I. , Journal Of Inorganic Biochemistry, Jun, Volume {98}, Number {5}, 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA, p.{833-840}, (2004) 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 [S2MoS2CuS2MoS2] [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 MoS42- 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. (C) 2003 Elsevier Inc. All rights reserved.

B
Bacterioferritin from Desulfovibrio vulgaris Hildenborough is a functional DPS-like enzyme, Folgosa, F., Timóteo C. G., Guilherme M., Penas D., Tavares P., and Pereira A. S. , FEBS JOURNAL, Sep, Volume {279}, Number {1, SI}, p.{465}, (2012) Abstract
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Biochemical and spectroscopic characterization of overexpressed fuscoredoxin from Escherichia coli, Pereira, A. S., Tavares P., Krebs C., Huynh B. H., Rusnak F., Moura I., and Moura J. J. G. , Biochemical And Biophysical Research Communications, Volume {260}, Number {1}, p.{209-215}, (1999) Abstract

Fuscoredoxin is a unique iron containing protein of yet unknown function originally discovered in the sulfate reducers of the genus Desulfovibrio. It contains two iron-sulfur clusters: a cubane [4Fe-4S] and a mixed oxo- and sulfide-bridged 4Fe cluster of unprecedented structure. The recent determination of the genomic sequence of Escherichia coli (E. coli) has revealed a homologue of fuscoredoxin in this facultative microbe. The presence of this gene in E. coli raises interesting questions regarding the function of fuscoredoxin and whether this gene represents a structural homologue of the better-characterized Desulfovibrio proteins. In order to explore the latter, an overexpression system for the E. coli fuscoredoxin gene was devised. The gene was cloned from genomic DNA by use of the polymerase chain reaction into the expression vector pT7-7 and overexpressed in E. coli BL21(DE3) cells. After two chromatographic steps a good yield of recombinant protein was obtained (approximately 4 mg of pure protein per liter of culture). The purified protein exhibits an optical spectrum characteristic of the homologue from D. desulfuricans, indicating that cofactor assembly was accomplished. Iron analysis indicated that the protein contains circa 8 iron atoms/molecule which were shown by EPR and Mossbauer spectroscopies to be present as two multinuclear clusters, albeit with slightly altered spectroscopic features. A comparison of the primary sequences of fuscoredoxins is presented and differences on cluster coordination modes are discussed on the light of the spectroscopic data. (C) 1999 Academic Press.