Desulfovibrio desulfuricans

Although the process requires the addition of a phosphate donor, such as glycerol-2-phosphate, it may be a valuable tool for cleaning water contaminated with radionuchdes. An alternative mode of uranium precipitation is driven by sulfate-reducing bacteria such as Desulfovibrio desulfuricans which reduce U(VI) to insoluble U(IV). When combined with bicarbonate extraction of contaminated soil, this may provide an effective treatment for removing uranium from contaminated soil (85). 

A Second Fepr Protein from Desulfovibrio desulfuricans... 

Sequence Comparison Between the N-Terminal Part of the Fepr Genes from Desulfovibrio desulfuricans (Dd) and Desulfovibrio vulgaris (Dv), Carbon Monoxide Dehydrogenase from Methanothrix soehngenii (Ms), Methanosarcina frisia Gdl (Mf), Clostridium thermoaceticum (Ct), Rhodospirillum rubrum (Rr), and Anaerobic Ribonucleotide Reductase from Escherichia coli (Ec) ... 

Seitz H-J, H Cypionka (1986) Chemolithotrophic growth of Desulfovibrio desulfuricans with hydrogen coupled to ammonification with nitrate or nitrite. Arch Microbiol 146 63-67. 

Choi S-C, TT Chase, R Bartha (1994) Metabolic pathways leading to mercury methylation in Desulfovibrio desulfuricans LS. Appl Environ Microbiol 60 4072-4077. 

Dwyer DF, JM Tiedje (1986) Metabolism of polyethylene glycol by two anaerobic bacteria, Desulfovibrio desulfuricans and a Bacteroides sp. Appl Environ Microbiol 52 852-856. 

Smock AM, ME Bottcher, H Cypionka (1998) Fractionation of sulfur isotopes during thiosulfate reduction by Desulfovibrio desulfuricans. Arch Microbiol 169 460-463. 

FIGURE 12.3 S = 9/2 EPR of Desulfovibrio desulfuricans hybrid cluster protein. Note the weak low-field peak with g > 14 and the relatively strong intensities in the g 5.4 and g 6.4 regions, which are all characteristics of the S = 9/2 system. 

Yoo ES, Libra J, Wiesmannn U (2000) Reduction of azo dyes by Desulfovibrio desulfuricans. Water Sci Technol 41 15-22... 

For the cytochrome c-plastocyanin complex, the kinetic effects of cross-linking are much more drastic while the rate of the intracomplex transfer is equal to 1000 s in the noncovalent complex where the iron-to-copper distance is expected to be about 18 A, it is estimated to be lower than 0.2 s in the corresponding covalent complex [155]. This result is all the more remarkable in that the spectroscopic and thermodynamic properties of the two redox centers appear weakly affected by the cross-linking process, and suggests that an essential segment of the electron transfer path has been lost in the covalent complex. Another system in which such conformational effects could be studied is the physiological complex between tetraheme cytochrome and ferredoxin I from Desulfovibrio desulfuricans Norway the spectral and redox properties of the hemes and of the iron-sulfur cluster are found essentially identical in the covalent and noncovalent complexes and an intracomplex transfer, whose rate has not yet been measured, takes place in the covalent species [156]. 

Desulfomicrobium baculatum D. baculatum formerly Desulfovibrio desulfurican strain Norway 4... 

Hatchikian, E. C., Magro, V., Eorget, N. and Nicolet, Y. (1999) Carboxy-terminal processing of the large subunit of [Ee] hydrogenase from Desulfovibrio desulfuricans ATCC 7757. J. Bacterial., 181, 2947-52. 

Matias, P. M., Soares, C. M., Saraiva, L. M., Coelho, R., Morais, J., LeGall, J. and Carrondo, M. A. (2001) [NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774 gene sequencing, three-dimensional structure determination and refinement at 1.8 angstrom and... 

Nicolet, Y., Piras, C., Legrand, P., Hatchikian, C. E. and Fontecilla-Camps, J. C. (1999) Desulfovibrio desulfuricans iron hydrogenase The structure shows unusual coordination to an active site Fe binuclear center. Structure Fold. Des., 7, 13-23. 

Argyle JL, Rapp-Giles BJ, Wall JD. 1992. Plasmid transfer by conjugation in Desulfovibrio desulfuricans. FEMS Microbiol Lett 94 255-62. 

Barton LL, editor. 1995. Sulfate-reducing bacteria. New York Plenum Press. Blanchard L, Marion D, Pollock B, et al. 1993. Overexpression of Desulfovibrio vulgaris Hildenborough cytochrome C553 in Desulfovibrio desulfuricans G200 evidence of conformational heterogeneity in the oxidized protein by NMR. Eur J Biochem 218 293-301. 

Rapp-Giles BJ, Casalot L, English RS, et al. 2000. Cytochrome mutants of Desulfovibrio desulfuricans. Appl Environ Microbiol 66 671-7. 

Wall ID, Mnrnan T, Argyle J, et al. 1996. Transposon mntagenesis in Desulfovibrio desulfuricans development of a random mutagenesis tool from Tn7. Appl Environ Microbiol 62 3762-7. 

Wall ID, Rapp-Giles BJ, Ronsset M. 1993. Characterization of a small plasmid from Desulfovibrio desulfuricans and its nse for shnttle vector construction. J Bacteriol 175 4121-8. 

Matias PM, Coelho R, Pereira lA, et al. 1999. The primary and three-dimensional structures of a nine haem cytochrome c from Desulfovibrio desulfuricans ATCC 2111A reveal a new member of the Hmc family. Structure 7 119-30. 

Moura I, Tavares P, Moura JJ, et al. 1990. Purification and characterization of desul-foferrodoxin. A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center. J Biol Chem 265 21596-602. 

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