Journal
ARCHIVES OF MICROBIOLOGY
Volume 176, Issue 4, Pages 306-309Publisher
SPRINGER-VERLAG
DOI: 10.1007/s002030100329
Keywords
sulfate-reducing bacteria; aerobic respiration; terminal oxidase; cytochrome c(3); periplasm; hydrogen; TMPD; ascorbate; Desulfovibrio vulgaris strain Marburg Desulfovibrio desulfuricans strain CSN Desulfovibrio termitidis strain KH1
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Washed cells of Desulfovibrio vulgaris strain Marburg (DSM 2119) reduced oxygen to water with H, as electron donor at a mean rate of 253 nmol O-2 min(-1) (mg protein)(-1). After separating the periplasm from the cells, more than 60% of the cytochrome c activity and 90% of the oxygen-reducing activity were found in the periplasmic fraction. Oxygen reduction and the reduction of cytochrome c with H, were inhibited by CuCl2. After further separation of the periplasm by ultrafiltration (exclusion sizes 30. 50, and 100 kDa), oxygen reduction with H-2 occurred with the retentates only. Ascorbate plus tetramethyl-p-phenylenediamine (TMPD), however, were also oxidized by the filtrates. The stoichiometry of 1 mol O-2 reduced per 2 mol ascorbate oxidized indicated the formation of water. Our experiments present evidence that in D. vulgaris periplasmic hydrogenase and cytochrome c play a major role in oxygen reduction. Preliminary studies with other Desulfovibrio species indicated a similar function of periplasmic c-type cytochromes in D. desulfuricans CSN and D. termitidis KH1.
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