Deep Sea Research Part I: Oceanographic Research Papers. Replot of the Vmax,app values derived from the curves shown in (A) versus ferricyanide concentration.C. DsrL mediates electron transfer between NADH and rDsrAB in Allochromatium vinosum. The apparent molecular mass of the enzyme was determined to be 30 kDa by gel filtration chromatography on Sephadex 75. In P. pantotrophus SoxY is believed to be the active site of protein‐bound sulphur oxidation (Quentmeier and Friedrich, 2001). Strain MED193 during Growth with Thiosulfate. Allochromatium vinosum wild‐type and mutant strains were characterized in batch culture experiments essentially as described in Prange et al. Elemental sulphur and tetrathionate were determined colorimetrically by cyanolysis (Kelly et al., 1969). Combined fractions containing the enzyme were dialysed against 20 mM TrisHCl, pH 7.5 and loaded onto DEAE Sephacel (Amersham Pharmacia Biotech, Uppsala, diameter 2.6 cm, 30 ml gel volume) equilibrated with the same buffer. The Sox system is found in green sulphur bacteria like C. tepidum as well as in different groups of Proteobacteria and the thermophilic bacterium Aquifex aeolicus (Petri et al., 2001; Friedrich et al., 2005). It has been a very long‐held conviction that the observed cleavage is brought about by the action of rhodaneses or thiosulphate reductases (Brune, 1989; 1995a; Dahl, 1999; Brüser et al., 2000). RNA Stabilization Directly and Comprehensively Revealed Episymbiotic Microbial Communities of Deep-Sea Squat Lobsters Metabolism of Inorganic Sulfur Compounds in Purple Bacteria. 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. Shown are representatives of triplicate experiments. Gene inactivation and complementation experiments proved these proteins to be indispensable for thiosulphate oxidation to sulphate. The supernatant was subjected to a Phenyl‐Sepharose matrix (diameter 2.6 cm, 50 ml gel volume) equilibrated with 1.2 M (NH4)2SO4 in 20 mM TrisHCl, pH 7.5. We have also demonstrated that the Sox system in this sulphur‐forming purple sulphur bacterium operates differently from that of the well‐studied chemotrophic and phototrophic α‐Proteobacteria (Mukhopadhyaya et al., 2000; Appia‐Ayme et al., 2001; Friedrich et al., 2001; 2005; Kappler et al., 2001). The column was calibrated using standard proteins (see above). We conclude that this protein is a contamination of thiosulphate dehydrogenase that we could not completely remove from our preparations. The air‐oxidized spectrum is represented by the solid line, while the thiosulphate‐reduced spectrum is represented by the dotted line. ΔG0′ for the electron‐donating, formally hydrogen‐forming reaction is +84.5 kJ mol−1 (Thauer et al., 1977). Structural analyses of the interactions of SoxY and SoxZ from thermo-neutrophilic Hydrogenobacter thermophilus. Standard methods were used for molecular biological techniques (Sambrook et al., 1989; Ausubel et al., 1997). Amino acid sequence of tryptic peptide fragments, their predicted Encyclopedia of Inorganic and Bioinorganic Chemistry. The corresponding fractions were combined, concentrated to keep the total volume below 2 ml, and further purified by gel filtration on Superdex TM200 equilibrated with gel filtration‐stabilizing buffer (50 mM TrisHCl, 2 mM sodium thiosulphate, 1 mM magnesium sulphate, 1 μM PMSF, pH 7.5) containing 150 mM NaCl (flow rate 0.5 ml min−1). For further purification of SoxXA and SoxB the appropriate protein containing fractions were combined, dialysed overnight against MonoQ‐stabilizing buffer (10 mM TrisHCl, 2 mM sodium thiosulphate, 1 mM magnesium sulphate, 1 μM PMSF, pH 7.5) and loaded onto MonoQ HR 5/5 equilibrated with the same buffer. While the product of ORFa could theoretically be involved in regulation of sox genes, the ccmA/ccmB gene products (Thöny‐Meyer et al., 1995) might play a role in maturation of the haem c‐containing Sox proteins SoxX and SoxA. The Structure and Function of Nervous Tissue. Denatured proteins were separated by SDS‐PAGE using the method of Laemmli (1970), followed by Coomassie blue or silver staining. Any queries (other than missing content) should be directed to the corresponding author for the article. Our first aim was therefore to find whether the proteins predicted by the sox genes are indeed produced in A. vinosum and, if so, to obtain information about their structure and properties. Aerobic desulfurization of biogas by acidic biotrickling filtration in a randomly packed reactor. Clusters of sox genes very similar to those of A. vinosum have been identified in the only distantly related green sulphur bacteria. Native and SDS‐PAGE analysis of thiosulfate kururiensis subsp. nov., a facultative chemolithoautotrophic thiosulfate oxidizing bacterium isolated from rhizosphere soil and proposal for classification of the type strain of Burkholderia kururiensis as Burkholderia kururiensis subsp. The Extracellular Space in the Vertebrate Central Nervous System. Differences in tolerance to mescaline produced by peripheral and direct central administration. In the sulphur‐storing A. vinosum we identified five sox genes in two independent loci (soxBXA and soxYZ). This is demonstrated by the lack of SoxA encoded downstream of the ΩKm insertion site in the soxXΩKm and ΔsoxBXΩKm mutants (Fig. Biochimica et Biophysica Acta (BBA) - Bioenergetics. . Western blot analysis was performed with antibodies against the indicated proteins SoxA, SoxB and SoxYZ. In the 325 bp intergenic region two putative promoter sequences were identified: the putative soxB promoter is situated 72 bp upstream of the corresponding start codon, the putative soxX promoter is located 244 bp upstream of the corresponding start codon. In their absence the latter is instead transferred to growing sulphur globules. Tetrathionate production by sulfur oxidizing bacteria and the role of tetrathionate in the sulfur cycle of Baltic Sea sediments, Sirohaem‐sulfite reductase and other proteins encoded in the, Quantitative speciation of sulfur in bacterial sulfur globules: X‐ray absorption spectroscopy reveals at least three different speciations of sulfur, The role of the sulfur globule proteins of, The cysteine residue of the SoxY protein as the active site of protein‐bound sulfur oxidation of, Detection of traces of oxidized and reduced sulfur compounds in small samples by combination of different high‐performance liquid chromatography methods, Parameters affecting transcription termination by, SoxRS‐mediated regulation of chemotrophic sulfur oxidation in, Small mobilizable multi‐purpose cloning vectors derived from the, Anaerobic oxidation of thiosulfate and elemental sulfur in, The enzymatic system thiosulfate: cytochrome, Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady‐state Enzyme Systems, A broad host range mobilization system for, The role of tetrathionate in the oxidation of thiosulphate by, Anaerobic oxidation of thiosulfate to tetrathionate by obligately heterotrophic bacteria, belonging to the, Oxidation of inorganic sulfur compounds: chemical and enzymatic reactions, Energy conservation in chemotrophic anaerobic bacteria, The role of thiosulfate in sulfur metabolism of, Sulphur metabolism in Thiorhodaceae.