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Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica

Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK¹
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK²

Author for correspondence: Ben C. Berks (at Oxford address). Tel: +44 1865 275250. Fax: +44 1865 275259. e-mail: ben.berks{at}bioch.ox.ac.uk

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.

Keywords: tetrathionate reductase, thiosulfate reductase, polysulfide reductase, molybdopterin, electron transport

Abbreviations: MGD, bis(molybdopterin guanine dinucleotide)molybdenum

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