Desulfovibrio vulgaris

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) ... 

Full details of the structure analysis and refinement are not appropriate to this review and will be published elsewhere, but it is hoped that sufficient information has been given to validate the unusual structure of the Fepr protein from Desulfovibrio vulgaris (Hilden-borough). 

A preliminaiy characterization of a new iron—sulfur protein isolated from Desulfovibrio vulgaris Hildenborough was reported in 1989 124). The protein contained approximately 6 iron and 6 inorganic sulfur atoms per molecule. The FPR spectrum of the dithionite reduced protein exhibited an S = signal similar to what was found for synthetic compounds with a [6Fe-6S] core (prismane core). No other FPR signals were reported at this time, and based on the observed similarity it was suggested that this peculiar iron-sulfur protein contained a [6Fe-6S] cluster. Because it had no known function, the pro-... 

Johnson MS, IB Zhulin, M-E R Gapuzan, BL Taylor (1997) Oxygen-dependent growth of the obligate anaerobe Desulfovibrio vulgaris Hildenborough. J Bacterial 179 5598-5601. 

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. 

Postgate (51) observed a high concentration of a type of cytochrome, designated cytochrome cz, in the strictly anaerobic sulfate-reducing bacterium, Desul/ovibrio. The cytochrome Cz Desulfovibrio vulgaris has been shown to possess a very low redox potential (—0.205 V), two heme groups per mole and a sequence which implies two half sections, each of which binds a heme group (52). 

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... 

FIGURE 5.14 Dual-mode 5 = 2 EPR from an iron protein. The T = 9 K spectra are from a mononuclear high-spin ferrous site in dithionite-reduced desulfoferrodox i n from Desulfovibrio vulgaris. The top trace was recorded in normal or perpendicular mode (5, L B0) the bottom trace was taken in parallel mode (IIt II B0). (Modified from Verhagen et al. 1993.)... 

FIGURE 6.3 Quantification on the first half of an isolated peak. The spectrum is from the [2Fe-2S] cluster in the enzyme adenosine phosphosulfate reductase from Desulfovibrio vulgaris (Verhagen et al. 1993). The inset shows the asymmetrical low-field -feature the vertical line at the peak position indicates the rightmost integration limit for quantification on half... 

FIGURE 7.4 Example of a spin-spin interaction spectrum. The complex spectrum is from two adjacent cubane clusters in the enzyme FeFe-hydrogenase from Desulfovibrio vulgaris. The lOOx blowup is to show the extended spectral field range resulting from interaction. 

FIGURE 13.6 Whole bacterial-cell EPR. A frozen concentrated suspension of cells from the sulfate-reducing bacterium Desulfovibrio vulgaris gives an EPR spectrum with only a [2Fe-2S]1+ signal and a flavin radical signal, both from adenosine phosphosulfate reductase. 

Pierik, A.J., Hagen, W.R., Dunham, W.R., and Sands, R.H. 1992a. Multi-frequency EPR and high-resolution Mossbauer spectroscopy of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough) characterization of a supercluster and superspin model protein. European Journal of Biochemistry 206 705-719. 

Verhagen, M.F.J.M., Kooter, I.M., Wolbert, R.B.G., and Hagen, W.R. 1993. On the iron-sulfur cluster of adenosine phosphosulfate reductase from Desulfovibrio vulgaris (Hildenborough). European Journal of Biochemistry 221 831-837. 

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]. 

Desulfovibrio indonensis Desulfovibrio vulgaris (Miyazaki) D. indonensis ... 

Berber, Y., Fauque, G. D., LeGall, J., Choi, E. S., Peck, H. D. Jr and Lespinat, P. A. (1987) Inhibition studies of three classes of Desulfovibrio hydrogenase Application to the further characterization of the multiple hydrogenases found in Desulfovibrio vulgaris Hildenborough. Biochem. Biophys. Res. Commun., 146, 147-53. 

Hagen, W. R., van Berkel-Arts, A., Kruse-Wolters, K. M., Dunham, W. R. and Veeger, C. (1986) EPR of a novel high-spin component in activated hydrogenase from Desulfovibrio vulgaris (Hildenborough). FEBS Lett., 201, 158-62. 

Higuchi, Y, Yasuoka, N., Kakudo, M., Katsube, Y, Yagi, T. and Inokuchi, H. (1987) Single crystals of hydrogenase from Desulfovibrio vulgaris Miyazaki P. J. Biol. Chem., 262, 2823-25. 

Higuchi, Y, Toujou, R, Tsukamoto, K. and Yagi, T. (2000) The presence of a SO molecule in [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki as detected by mass spectrometry (In Process Citation)./. Inorg. Biochem., 80, 205-11. 

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