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A molybdenum-containing (2Fe, 2S) protein from desulphovibrio gigas, a sulphate reducer, Moura, J. J. G., Xavier A. V., Bruschi M., Legall J., and Cabral J. M. P. , Journal of the Less Common Metals, Volume 54, Number 2, p.555-562, (1977) AbstractWebsite
A molybdenum-containing iron-sulphur protein from Desulphovibrio gigas, Moura, J. J., Xavier A. V., Bruschi M., Legall J., Hall D. O., and Cammack R. , Biochem Biophys Res Commun, Oct 4, Volume 72, Number 3, p.782-9, (1976) AbstractWebsite
Purification, characterization and biological activity of three forms of ferredoxin from the sulfate-reducing bacterium Desulfovibrio gigas, Bruschi, M., Hatchikian C., Legall J., Moura J. J., and Xavier A. V. , Biochim Biophys Acta, Nov 9, Volume 449, Number 2, p.275-84, (1976) AbstractWebsite

Three forms of ferredoxin FdI, FdI', and FdII have been isolated from Desulfovibrio gigas, a sulfate reducer. They are separated by a combination of DEAE-cellulose and gel filtration chromatographic procedures. FdI and FdI' present a slight difference in isoelectric point which enables the separation of the two forms over DEAE-cellulose, while FdII is easily separated from the two other forms by gel filtration. The three forms have the same amino acid composition and are isolated in different aggregation states. Molecular weight determinations by gel filtration gave values of 18 000 for FdI and FdI' and 24 000 for FdII, whereas a value of 6000 is determined when dissociation is accomplished with sodium dodecyl sulfate. The electronic spectra are different and their ultraviolet-visible absorbance rations are 0.77, 0.87 and 0.68 respectively for FdI, FdI' and FdII. Despite these differences, the physiological activities of the three forms are similar as far as the reduction of sulfite by molecular hydrogen is concerned.