1887

Abstract

The tetrathionate (Ttr) and thiosulfate (Phs) reductases of LT2, together with the polysulfide reductase (Psr) of , 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.

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2002-11-01
2020-04-02
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