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The tetrathionate (Ttr) and thiosulfate (Phs) reductases of Salmonella enterica LT2, together with the polysulfide reductase (Psr) of Wolinella succinogenes, are unusual examples of enzymes containing a molybdopterin active-site cofactor since all formally catalyse sulfur-sulfur bond cleavage. This is in contrast to the oxygen or hydrogen transfer reactions exhibited by other molybdopterin enzymes. Here the catalytic specificity of Ttr and Phs has been compared using both physiological and synthetic electron-donor systems. Ttr is shown to catalyse reduction of trithionate but not sulfur or thiosulfate. In contrast, Phs cannot reduce tetrathionate or trithionate but allows whole cells to utilize elemental sulfur as an electron acceptor. Mechanisms are proposed by which the bacterium is able to utilize an insoluble sulfur substrate by means of reactions at the cytoplasmic rather than the outer membrane.

Original publication

DOI

10.1099/00221287-148-11-3631

Type

Journal article

Journal

Microbiology

Publication Date

11/2002

Volume

148

Pages

3631 - 3638

Keywords

Amino Acid Sequence, Binding Sites, Catalysis, Cysteine, Molecular Sequence Data, Mutagenesis, Oxidation-Reduction, Oxidoreductases, Oxidoreductases Acting on Sulfur Group Donors, Respiration, Salmonella enterica, Sequence Homology, Amino Acid, Sulfur, Sulfur Acids, Sulfur Compounds, Sulfurtransferases