Allochromatium vinosum wild type readily oxidized added thiosulphate, resulting in the simultaneous production of sulphate and tetrathionate. Thiosulphate is a derived term of sulfate. DNA was sequenced by Sequiserve (Vaterstetten, Germany). Gel filtration yielded an apparent molecular mass of 38 kDa indicating that the protein is present as a monomer. To obtain plasmids for complementation of the soxXΩKm and ΔsoxY mutant, respectively, fragments of genomic DNA of A. vinosum containing the corresponding gene and potential upstream promoter sequences were cloned into the broad‐host‐range vector pBBR1 MCS‐2. A combined approach of 16S rRNA and a functional marker gene, soxB to reveal the diversity of sulphur-oxidising bacteria in thermal springs. As soxYZ are located independently from soxBXA in A. vinosum, the expression of these genes could be regulated in a different way. It is formed by oxidative condensation of two thiosulphate anions catalysed by thiosulphate dehydrogenase (EC 1.8.2.2; thiosulphate:acceptor oxidoreductase) (Trudinger, 1961). Bacterial sulfur globules: occurrence, structure and metabolism, Protein targeting to the bacterial cytoplasmic membrane, Interposon mutagenesis of soil and water bacteria: a family of DNA fragments designed for, Novel genes coding for lithotrophic sulfur oxidation of. Cytochrome c from yeast is used as electron acceptor by the enzyme, under optimized assay conditions (20 mM acetate buffer, pH 5.5, 0.4 mM thiosulphate, 25 μM yeast cytochrome c) the activity amounted to 230 μmol cytochrome c reduced min−1 (mg protein)−1. Accordingly, A. vinosum thiosulphate dehydrogenase was also proven to be a periplasmic c‐type cytochrome. Two different pathways appear to exist: in the first, both sulphur atoms of thiosulphate are oxidized to sulphate without the appearance of sulphur deposits as intermediates. oxidoreductase from A. vinosum. With the exception of the soxA‐encoded cytochrome c551 from C. limicola (Vertéet al., 2002) biochemical information about sox‐encoded proteins from sulphur‐storing organism has so far not been available. Ecological roles of dominant and rare prokaryotes in acid mine drainage revealed by metagenomics and metatranscriptomics. 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. Plasmid transfer was performed in electrotransformation cuvettes of 2 mm width using a Gene Pulser II with a Pulse Controller Plus (Bio‐Rad, München). In contrast, in A. vinosum soxBXA and soxYZ are located on two independent sites on the genome, thereby preventing co‐transcription. It exhibits similarity to amino acids 28–67 of a hypothetical c‐type cytochrome from Ralstonia metallidurans (Accession No. However, in organisms like A. vinosum that lack the ‘sulphur dehydrogenase’ SoxCD the sulphane sulphur atom still hooked up to SoxY cannot be directly further oxidized. Inorganic sulfur oxidizing system in green sulfur bacteria. The −10 box is located 299 bp upstream of the soxY start codon. Each reaction contained 50 μl of cell solution and 0.1–0.5 μg of purified plasmid DNA. The time constant τ should be about 5 ms under the chosen conditions. Water-soluble, Its solubility at 100° C is 231 g/100 ml of vapour. Second, we proved the formation of trithionate and pentathionate in the cultures by HPLC.