Desulfovibrio bacteria

Figure 4-459. Diagram of the bacterial corrosion of steel or iron by Desulfovibrio bacteria (corrosion products are underlined). (From Ref. [208].)...

Lactate is also involved in overall sulfate reduction reactions such as these employed by the Desulfovibrio bacteria. One such reaction is given by (Decker et al. 1970)... 

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). 

Sulfate reducers. The best-known form of microbiologically influenced corrosion involves sulfate-reducing bacteria.- Without question, sulfate reducers cause most localized industrial cooling water corrosion associated with bacteria. Desulfovibrio, Desulfomonas, and Desulfotomacu-lum are three genera of sulfate-reducing bacteria. 

This key enzyme of the dissimilatory sulfate reduction was isolated from all Desulfovibrio strains studied until now 135), and from some sulfur oxidizing bacteria and thermophilic Archaea 136, 137). The enzymes isolated from sulfate-reducing bacteria contain two [4Fe-4S] clusters and a flavin group (FAD) as demonstrated by visible, EPR, and Mossbauer spectroscopies. With a total molecular mass ranging from 150 to 220 kDa, APS reductases have a subunit composition of the type 012)32 or 02)3. The subunit molecular mass is approximately 70 and 20 kDa for the a and )3 subunits, respectively. Amino-acid sequence data suggest that both iron-sulfur clusters are located in the (3 subunit... 

Sulfate reducing bacteria of the genus Desulfovibrio are one of the main sources of enzyme. Hydrogenases can be found in different sites in the bacterial cell periplasm, cytoplasm, and membrane. A given species may have hydrogenases in one or in several of these cell sites. 

Although reduction of chromate Cr to Cr has been observed in a number of bacteria, these are not necessarily associated with chromate resistance. For example, reduction of chromate has been observed with cytochrome Cj in Desulfovibrio vulgaris (Lovley and Phillips 1994), soluble chromate reductase has been purified from Pseudomonas putida (Park et al. 2000), and a membrane-bound reductase has been purified from Enterobacter cloacae (Wang et al. 1990). The flavoprotein reductases from Pseudomonas putida (ChrR) and Escherichia coli (YieF) have been purified and can reduce Cr(VI) to Cr(III) (Ackerley et al. 2004). Whereas ChrR generated a semi-quinone and reactive oxygen species, YieR yielded no semiquinone, and is apparently an obligate four-electron reductant. It could therefore present a suitable enzyme for bioremediation. 

Nanninga HJ, JC Gottschal (1987) Properties of Desulfovibrio carbinolicus sp. nov. and other sulfate-reducing bacteria isolated from an anaerobic-purification plant. Appl Environ Microbiol 53 802-809. 

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. 

Rubrerythrin is the trivial name given to a family of non-haem iron proteins that have been isolated from a number of bacteria (Figure 6.2). The structure of the best characterized rubrerythrin, that from Desulfovibrio vulgaris, has been determined by... 

Although electron transfers in biological systems are generally expected to be non-adiabatic, it is possible for some intramolecular transfers to be close to the adiabatic limit, particularly in proteins where several redox centers are held in a very compact arrangement. This situation is found for example in cytochromes C3 of sulfate-reducing bacteria which contain four hemes in a 13 kDa molecule [10, 11], or in Escherichia coli sulfite reductase where the distance between the siroheme iron and the closest iron of a 4Fe-4S cluster is only 4.4 A [12]. It is interesting to note that a very fast intramolecular transfer rate of about 10 s was inferred from resonance Raman experiments performed in Desulfovibrio vulgaris Miyazaki cytochrome Cj [13]. 

Odom, J. M. and Peck, H. D. (1984) Hydrogenase, electron-transfer proteins, and energy coupling in the sulfate reducing bacteria Desulfovibrio. Ann. Rev. Microbiol., 38, 551. 

By interesting coincidence, the old dogma that cytochromes are not present in anaerobes was demolished by discovery, at about the same time, of c-type cytochromes in Desulfovibrio and anoxygenic photosynthetic bacteria (Kamen and Vernon 1955). 

Peck then became interested in sulfate-reducing bacteria, which he had got to know in Gest s laboratory. To study the reduction of sulfate. Peck worked in Fritz Lipmann s laboratory in Massachussetts General Hospital (1956) and with Lipmann at Rockefeller University (1957). Lipmann started work on active sulfate in 1954 with Helmut Hilz as a postdoctoral fellow and studied the activation of sulfate to APS and PAPS. Lipmann had left the active sulfate projects by 1957 and started, at Rockefeller University, the studies on protein synthesis. Peck published one paper on the reduction of sulfate with hydrogen in extracts of Desulfovibrio desul-furicans (1959) and one on APS as an intermediate on the oxidation of thiosulfate by Thiobacillus thioparus (1960). 

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. 

Odom JM, Peck HD Jr. 1981. Hydrogen cycling as a general mechanism for energy coupling in the sulfate-reducing bacteria, Desulfovibrio sp. FEMS Microbiol Lett 12 47-50. 

Evidence for an alternative oxidative stress protection mechanism in sulfate-reducing bacteria has begun to emerge. Table 10.1 provides data on the proteins implicated in this alternative system. All but one of these proteins contain distinctive types of nonheme iron active sites. This chapter describes recent results on three of these novel proteins DcrH, Rbo, and Rbr, all from Desulfovibrio vulgaris HUdenborough. 

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