Wolinella succinogenes

The conditions under which these function and their regulation depend on the organism. For example, in Escherichia coli, oxygen represses the synthesis of the other reductases, and under anaerobic conditions the reductases for fumarate, DMSO, and TMAO are repressed by nitrate. This does not apply to Wolinella succinogenes in which sulfur represses the synthesis of the more positive electron acceptors nitrate and fumarate (Lorenzen et al. 1993). The DMSO reductase from Escherichia coli (Weiner et al. 1988) has a broad substrate versatility, and is able to reduce a range of sulfoxides and A-oxides. Anaerobic sulfate reduction is not discussed here in detail. 

The existence of microaerophilic organisms such as Wolinella succinogenes that was formerly considered an anaerobe or, conversely, the oxygen tolerance of many Clostridia, suggests that such organisms may occupy an ecological niche between the two extremes already noted. 

Figure 13.16 (a) Polypeptide fold and (b) electron transfer distances in E. coli quinol-fumarate reductase, (c) intercofactor distances in the Wolinella succinogenes enzyme. (From Iverson et al., 2002. Reproduced by permission of the Journal of Biological Chemistry.)... 

Albracht, S. P. J., Kroger, A., Van der Zwaan, J. W., Unden, G., Bocher, R., Mell, H. and Fontijn, R. D. (1986) Direct evidence for sulfur as a ligand to nickel in hydrogenase An EPR study of the enzyme from Wolinella succinogenes enriched in O2. Biochim. Biophys. Acta, 874, 116-27. 

The general nature of the Tat system became apparent when it was found that FdhA, the catalytic subunit of formate dehydrogenase from Wolinella succinogenes, also has a twin-arginine signal peptide (Bokrantz et al. 1991)... 

Lorenzen J, Steinwachs S, Unden G. 1994. DMSO respiration by the anaerobic bacterium Wolinella succinogenes. Arch Microbiol 162 277-81. 

Selenium, in the form of selenate or selenite, is toxic to D. desulfuricans (Tomei et al. 1995) and Wolinella succinogenes (Tomei et al. 1992) at elevated levels. At sublethal levels of 0.1-1. OmM selenite or 10 mM selenate, minimal levels of growth is observed with both D. desulfuricans and Wolinella succinogenes. With both selenate and selenite, colloidal elemental selenium (Se°) is produced inside the cell and released into the culture fluid after cell death. This reduction of Se(VI) and Se(IV) by these anaerobes is not coupled to growth and proceeds by mechanisms that have not yet been identified. Selenite and selenate reduction with formation of elemental selenium by these nonrespiratory processes serve to detoxify the environment for future bacteria and may be important for the geochemical cycle of selenium. 

Tomei FA, Barton LL, Lemanski CL, Zocco TG. 1992. Reduction of selenate and selenite to elemental selenium by Wolinella succinogenes. Can J Microbiol 38 1328-33. 

Blackmore, R., Roberton, A. M., and Brittain, T. (1986). The purification and some equilibrium properties of the nitrite reductase of the bacterium Wolinella succinogenes. Biochem. J. 233, 547-552. 

Payne, W. J., Grant, M. A., Shapleigh, J., and Hoffman, P. (1982). Nitrogen oxide reduction in Wolinella succinogenes and Campylobacter species. J. Bacterial. 152, 915-918. 

Teraguchi, T., and Hollocher, T. C. (1989). Purification and some characteristics of a cytochrome c-containing nitrous oxide reductase from Wolinella succinogenes. ]. Biol. Chem. 264, 1972-1979. 

THE STRUCTURE OF Wolinella succinogenes QUINOL FUMARATE REDUCTASE AND ITS RELEVANCE TO THE SUPERFAMILY OF SUCCINATE QUINONE OXIDOREDUCTASES... 

VIII. Electron and Proton Transfer and the Wolinella succinogenes Paradox. 142... 

Wolinella succinogenes QFR subunit A, of 73 kDa (Lauterbach et al., 1990), is composed of four domains (Fig. 3a, see color insert), the bipartite FAD binding domain (blue, residues Al-260 and A366-436, with A ... 

Reductive cleavage of sulfur-sulfur bonds in inorganic sulfur species is exploited in terminal electron transfer in some bacteria. The tetrathionate and thiosulfate reductases of the enteric bacterium Salmonella enterica LT2 and the polysulfide reductase of the rumen bacterium Wolinella succinogenes effect such reactions. ... 

Figure 9 Structure of NrfA dimer from (a) Wolinella succinogenes (PDB code 1FS7) and (b) D. desulfuricans ATCC27774 (PDB code lOAH) ...

This is a remarkable reaction because the transition metal chemistry of N2O is sparse, especially with copper. Most N2O reductases are soluble, periplasmic homodimers however, there are examples of membrane-associated enzymes. " The best characterized N2O reductases are from Paracoccus denitrificans, Pseudomonas nautica, and Pseudomonas stutzeri, and most of the information presented here is derived from experiments on these enzymes. Where comparable data are available, N2O reductases from various organisms appear to be fairly similar, with the exception of the enzyme from Wolinella succinogenes, as noted above. The crystal stractmes of N2O reductase from P. nautica and more recently from P. denitrificans show two distinct copper clusters per subunit a bis-thiolate bridged dinuclear electron-transfer site (Cua), which is analogous to the Cua site in cytochrome c oxidase see Cyanide Complexes of the Transition Metals), and a novel four-copper cluster ligated by seven histidines, the catalytic copper site (Cuz), where N2O is thought to bind and be reduced. Cuz was proposed to be a copper-histidine cluster on the basis of the presence of nine strictly conserved histidine residues, and this was supported by a H NMR study that identified two non-CuA associated resonances that were assigned as copper-histidine N-H protons. ... 

Kaden J., Galushko A. S., and Schink B. (2002) Cysteine-mediated electron transfer in syntrophic acetate oxidation by co-cultures of Geobacter sulfurreducens and Wolinella succinogenes. Arch. Microbiol. 178, 53—58. 

A sulfur reductase has been obtained from a heterotroph, Wolinella succinogenes (Schroder et al., 1988). This sulfur reductase has molecular mass of 200 kDa (made up of 85 kDa subunits) and an Fe/S cluster, but no heme. The enzyme catalyzes the oxidation of formate with elemental sulfur in the presence of formate dehydrogenase. As formate dehydrogenase used here has cytochrome b, the sulfur-reducing system of the bacterium is said to include cytochrome b. 

Schroder I, Kroger A, Nacy JM (1988) Isolation of the sulphur reductase and reconstitution of the sulphur respiration of Wolinella succinogenes. Arch Microbiol 149 572-579 Servent D, Delaforge M, Ducrocq C, Mansuy D, Lenfant M (1989) Nitric oxide formation during microsomal hepatic denitration of glyceryl trinitrate involvement of cytochrome P-450. Biochem Biophys Res Commun 163 1210-116... 

The conditions under which these function and their regulation depend on the organism. For example, whereas in E. coli, oxygen represses the synthesis of the other reductases, and under anaerobic conditions the reductases for fumarate, DMSO, and TMAO are repressed by nitrate, this is not the case for Wolinella succinogenes... 

A monoheme protein has also been isolated from the denitrifier Wolinella succinogenes [38]. This soluble c-type cytochrome of 8.2 kDa has a reduction potential of 105 mV at pH 7.6, and displays a spin equilibrium in the ferric form between a five-coordinate high-spin form and a low-spin one, where methionine occupies the sixth coordination position. 

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