Molecular Properties of the Dissimilatory Sulfite Reductase from <i>Desulfovibrio Desulfuricans</i> (Essex) and Comparison with the Enzyme from <i>Desulfovibrio Vulgaris</i> (Hildenborough)

Steuber, Julia; Arendsen, A.F.; Hagen, Wilfred R.; Kroneck, Peter M. H.

doi:10.1111/j.1432-1033.1995.873_3.x

Cited by 56 publications

(41 citation statements)

References 40 publications

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“…We detected three subunits, ␣ (49 kDa), ␤ (53 kDa), and ␥ (11 kDa) (Fig. 2), and we interpret the native structure to be ␣ 2 ␤ 2 ␥ n (n Ն 2), as suggested for D. desulfuricans Essex 6 (40). The function of the 11-kDa ␥ subunit that was copurified in most sulfite reductases (36) except that from A. fulgidus (9) is not clear at present.…”

Section: Discussionmentioning

confidence: 93%

“…The function of the 11-kDa ␥ subunit that was copurified in most sulfite reductases (36) except that from A. fulgidus (9) is not clear at present. Whereas Pierik et al reported that the ␥ subunit was tightly associated in the DSR of D. vulgaris (36), it was shown that in D. desulfuricans Essex 6, this subunit can be separated during gel filtration, which indicated a less tight association of DsrC with the ␣ and ␤ subunits in that organism (40). The presence and position of the putative promoter 123 nucleotides upstream of the translational start of the dsrA gene and putative termination sequences downstream of the stop codon of dsrB indicate that dsrA and dsrB constitute a single transcription unit and that the genes are coordinately expressed.…”

Section: Discussionmentioning

confidence: 99%

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Dissimilatory Sulfite Reductase (Desulfoviridin) of the Taurine-Degrading, Non-Sulfate-Reducing Bacterium Bilophila wadsworthia RZATAU Contains a Fused DsrB-DsrD Subunit

et al. 2001

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A dissimilatory sulfite reductase (DSR) was purified from the anaerobic, taurine-degrading bacterium Bilophila wadsworthia RZATAU to apparent homogeneity. The enzyme is involved in energy conservation by reducing sulfite, which is formed during the degradation of taurine as an electron acceptor, to sulfide. According to its UV-visible absorption spectrum with maxima at 392, 410, 583, and 630 nm, the enzyme belongs to the desulfoviridin type of DSRs. The sulfite reductase was isolated as an ␣ 2 ␤ 2 ␥ n (n > 2) multimer with a native size of 285 kDa as determined by gel filtration. We have sequenced the genes encoding the ␣ and ␤ subunits (dsrA and dsrB, respectively), which probably constitute one operon. dsrA and dsrB encode polypeptides of 49 (␣) and 54 kDa (␤) which show significant similarities to the homologous subunits of other DSRs. The dsrB gene product of B. wadsworthia is apparently a fusion protein of dsrB and dsrD. This indicates a possible functional role of DsrD in DSR function because of its presence as a fusion protein as an integral part of the DSR holoenzyme in B. wadsworthia. A phylogenetic analysis using the available Dsr sequences revealed that B. wadsworthia grouped with its closest 16S rDNA relative Desulfovibrio desulfuricans Essex 6.Bilophila wadsworthia is a strictly anaerobic, gram-negative bacterium (2) which belongs to the family Desulfovibrionaceae in the delta subdivision of the Proteobacteria, but does not reduce sulfate (2, 25). B. wadsworthia has been found quite frequently in patients with appendicitis and its complications and is the third most common anaerobic isolate in such infections (11), but can also be isolated from a wide variety of other infections, e.g., biliary tract infection (41), liver abscess (41), and ear infections (39). B. wadsworthia has also been found in the normal fecal flora (2). The organism lacks classical virulence factors like capsules, fimbriae, and extracellular enzymes (2). However, preliminary studies have indicated that B. wadsworthia exerts cytotoxic effects on two cell lines, and endotoxic activity of B. wadsworthia has been described (2, 34).We recently isolated from a communal sewage plant a strain of B. wadsworthia which utilizes organic sulfonates (e.g., taurine [2-aminoethanesulfonate]) as a carbon source and electron sink. B. wadsworthia respires taurine anaerobically with electrons derived mainly from formate oxidation and oxidation of the taurine carbon (25). Taurine is transaminated to sulfoacetaldehyde (22), which is cleaved to sulfite and an unidentified organic product (K. Denger and A. M. Cook, unpublished). Finally, sulfite is reduced to sulfide by a dissimilatory sulfite reductase (DSR) (6, 25). In addition, sulfite or thiosulfate serves as an electron acceptor for anaerobic respiration with formate as the electron donor in B. wadsworthia (25).DSR, a key enzyme in dissimilatory sulfate reduction, occurs in all organisms capable of reducing sulfite during anaerobic respiration investigated so far (9, 33). Otherwise, DSRs are rare....

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Section: Discussionmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Dissimilatory Sulfite Reductase (Desulfoviridin) of the Taurine-Degrading, Non-Sulfate-Reducing Bacterium Bilophila wadsworthia RZATAU Contains a Fused DsrB-DsrD Subunit

et al. 2001

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“…In common with other Dsrs, the enzyme has an a 2 b 2 structure and contains siroheme, nonheme iron, and acid-labile sulfur [36]. An additional protein with an apparent molecular mass of 11 kDa is associated with sulfite reductase from D. vulgaris [38] and Desulfovibrio desulfuricans [39,40]. The function of this so called c subunit is not yet known.…”

Section: Discussionmentioning

confidence: 99%

“…In most of the organisms that have been studied, the enzyme has been isolated from the soluble fraction. Sulfite reductase from D. desulfuricans was found to be partially membraneassociated after gentle disruption of the cells [39,40].…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea

Mander¹,

Duin²,

Linder³

et al. 2002

Eur J Biochem

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“…The gene encoding DsrC (ORF8) was displayed in fosmids ws39f7 and ws7f8. DsrC was proposed to further reduce oxidized sulfur intermediates, such as thiosulfate (48,50). Both DsrC and DsrD are not essentially tightly associated with DsrAB (18,40).…”

Section: Resultsmentioning

confidence: 99%

Clustered Genes Related to Sulfate Respiration in Uncultured Prokaryotes Support the Theory of Their Concomitant Horizontal Transfer

et al. 2005

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The dissimilatory reduction of sulfate is an ancient metabolic process central to today's biogeochemical cycling of sulfur and carbon in marine sediments. Until now its polyphyletic distribution was most parsimoniously explained by multiple horizontal transfers of single genes rather than by a not-yet-identified "metabolic island." Here we provide evidence that the horizontal transfer of a gene cluster may indeed be responsible for the patchy distribution of sulfate-reducing prokaryotes (SRP) in the phylogenetic tree. We isolated three DNA fragments (32 to 41 kb) from uncultured, closely related SRP from DNA directly extracted from two distinct marine sediments. Fosmid ws39f7, and partially also fosmids ws7f8 and hr42c9, harbored a core set of essential genes for the dissimilatory reduction of sulfate, including enzymes for the reduction of sulfur intermediates and synthesis of the prosthetic group of the dissimilatory sulfite reductase. Genome comparisons suggest that encoded membrane proteins universally present among SRP are critical for electron transfer to cytoplasmic enzymes. In addition, novel, conserved hypothetical proteins that are likely involved in dissimilatory sulfate reduction were identified. Based on comparative genomics and previously published experimental evidence, a more comprehensive model of dissimilatory sulfate reduction is presented. The observed clustering of genes involved in dissimilatory sulfate reduction has not been previously found. These findings strongly support the hypothesis that genes responsible for dissimilatory sulfate reduction were concomitantly transferred in a single event among prokaryotes. The acquisition of an optimized gene set would enormously facilitate a successful implementation of a novel pathway.

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Molecular Properties of the Dissimilatory Sulfite Reductase from Desulfovibrio Desulfuricans (Essex) and Comparison with the Enzyme from Desulfovibrio Vulgaris (Hildenborough)

Cited by 56 publications

References 40 publications

Dissimilatory Sulfite Reductase (Desulfoviridin) of the Taurine-Degrading, Non-Sulfate-Reducing Bacterium Bilophila wadsworthia RZATAU Contains a Fused DsrB-DsrD Subunit

Dissimilatory Sulfite Reductase (Desulfoviridin) of the Taurine-Degrading, Non-Sulfate-Reducing Bacterium Bilophila wadsworthia RZATAU Contains a Fused DsrB-DsrD Subunit

Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea

Clustered Genes Related to Sulfate Respiration in Uncultured Prokaryotes Support the Theory of Their Concomitant Horizontal Transfer

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