However, the physiological role of these enzymes remained dubious. Behavior Research Methods & Instrumentation, Three sox‐encoded proteins were purified: the heterodimeric c‐type cytochrome SoxXA, the monomeric SoxB and the heterodimeric SoxYZ. For P. pantotrophus SoxYZ additional homodimeric and heterotetrameric states have been described (Quentmeier et al., 2003). Thiosulphate oxidation in A. vinosum wild type (◆) and the mutants soxXΩKm (◊), soxBΩKm (▴), soxBXΩKm (Δ) and ΔsoxY (▪). Purification of thiosulfate:acceptor The purification of SoxXA, SoxB and SoxYZ from A. vinosum DSM 180T was monitored using the appropriate antisera. Thiosulphate is a derived term of sulfate. Combined fractions containing the enzyme were loaded onto a pre‐packed MonoQ HR 5/5 column equilibrated with 20 mM TrisHCl, pH 7.5. Possibly, other sulphur transferases present in the cells function as a back‐up system. The pellet was washed three times in 2 ml of ice‐cold dimethyl sulphoxide (DMSO) solution [10% (v/v)], precipitated again (4°C, 5900 g, 10 min) and finally resuspended in 1 ml of the same solution. It was concluded: (a) that sulphate and thiosulphate, like iodide, were accumulated by choroid plexus in vitro by active transport; (b) that sulphate and thiosulphate share and compete for a transport mechanism which is separate from the iodide transport mechanism; and. As also reported for P. pantotrophus (Friedrich et al., 2000), the SoxX protein band exhibited a weaker Coomassie stain than SoxA, even though both subunits are present in a 1:1 ratio. The gill chamber epibiosis of deep‐sea shrimp imicaris exoculata: an in‐depth metagenomic investigation and discovery of etaproteobacteria. The expression of soxA and soxB, however, remained undisturbed. The end‐product of thiosulphate oxidation in the presence of ferricyanide as artificial electron acceptor by thiosulphate dehydrogenase was tetrathionate. A thiosulphate dehydrogenase is responsible for the oxidation to tetrathionate, while a sox gene‐encoded multienzyme complex is essential for the oxidation to sulphate. A SoxYZ heterodimer was also found for A. vinosum as the protein eluted in fractions from gel filtration chromatography corresponding to an apparent molecular mass of 24 kDa. Storage and turnover of thiosulphate sulphur in, Identification of a thiosulfate utilization gene cluster from the green phototrophic bacterium, Purification and characterization of a periplasmic thiosulfate dehydrogenase from the obligately autotrophic, Cloning and characterization of sulfite dehydrogenase, two. Experiments were started by the addition of 2 mM thiosulphate from a sterile filtered stock solution (0.4 M). For curves with n > 1 a substrate concentration [S]0.5 can be reported that yields half maximal velocity and is characteristic of the process. The A. vinosum soxBXA and soxYZ genes products exhibit higher sequence identities to those of the sulphur‐forming green sulphur bacteria (62–65% for SoxB, 50–51% for SoxA, 46–51% for SoxX, 48–52% for SoxY, 37–45% for SoxZ) and to those of the β‐Proteobacterium T. denitrificans (57% for SoxB, 43% for SoxA, 47% for SoxX, 55% for SoxY, 55% for SoxZ) than to those of the chemotrophic α‐proteobacterial model organism P. denitrificans (53% for SoxB, 30% for SoxA, 36% for SoxX, 41% for SoxY, 35% for SoxZ) and the phototrophic α‐Proteobacterium R. sulfidophilum (50% for SoxB, 30% for SoxA, 39% for SoxX, 43% for SoxY, 32% for SoxZ). Marichromatium litoris sp. The soxXΩKm, soxBΩKm and soxBXΩKm mutants carrying insertions of a polar Ω kanamycin resistance cassette all exhibited a significantly reduced rate of thiosulphate oxidation (Fig. Molecular Interactions, Structural Transitions and Alterations in SoxB Protein Due to SoxYZ Interaction from Two Distinct β-Proteobacteria: An In silico Approach Towards the Thiosulfate Oxidation and Recycling of SoxY Protein. Insight into the Conformational Variations in SoxYZ Protein Complex from Two Different Members of the β-Proteobacterial Family Involved in Sulfur Oxidation. The proteins are located in the periplasm, all except of SoxZ are predicted to be synthesized as precursors carrying signal peptides. Each reaction contained 50 μl of cell solution and 0.1–0.5 μg of purified plasmid DNA. New bacterial and archaeal lineages discovered in organic rich sediments of a large tropical Bay. For the purification of SoxYZ, chromatography on MonoQ was omitted. The effect of O2 and pressure on thiosulfate oxidation by Thiomicrospira thermophila. While tetrathionate formation remained unaffected (Fig. In the present study, two distinct enzyme systems for thiosulphate oxidation in A. vinosum have clearly been identified. To prove that the observed lack of sulphate formation from thiosulphate was indeed caused by inactivation of sox genes, two A. vinosum mutants, soxXΩKm and ΔsoxY, were complemented in trans. In addition to the proteins with significant similarity to Sox proteins from other organisms, the polypeptides deduced from two of the other sequenced genes deserve special attention: the protein encoded by ORF9 shows similarity to hypothetical proteins from the green sulphur bacteria Chlorobium limicola (strain Tassajara, DSM 249) as well as from Chlorobaculum (formerly Chlorobium; Imhoff, 2003) tepidum (strain TLS, DSM 12025T).


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