Oxidative phosphorylation linked to the dissimilatory reduction of elemental sulphur by Desulfovibrio.
Hydrogenase and cytochrome c3 purified from Desulfovibrio gigas and D. desulfuricans strain Norway form a soluble complex which is capable of transferring electrons from molecular hydrogen to colloidal sulphur (S0). In this reaction, sulphur is reduced to hydrogen sulphide. Since both strains are capable of growth using elemental sulphur as terminal electron acceptor, it was of interest to check for oxidative phosphorylation in this sulphur reduction sytem. Membranes isolated from D. gigas or D. desulfuricans strain Norway contain hydrogenase and c-type cytochromes and catalyse the H2 leads to S0 reaction. With D. gigas, esterification of orthophosphate is coupled to the membrane-mediated transfer of electrons from H2 to S0. A P/2e ratio of 0.1 was observed and this value could be reduced by the addition of colloidal sulphur with c2 may be more than a purely chemical reaction. Since whole cells can use sulphur flower while cell-free extracts react only with colloidal sulphur, it is evident that cells handle sulphur in a way which is not yet fully understood.
D000255:Adenosine Triphosphate / Q000096:biosynthesis; D003574:Cytochrome c Group / Q000378:metabolism; D003901:Desulfovibrio / Q000201:enzymology / Q000378:metabolism*; D006864:Hydrogenase; D010084:Oxidation-Reduction; D010085:Oxidative Phosphorylation / Q000187:drug effects*; D010088:Oxidoreductases / Q000378:metabolism; D013455:Sulfur / Q000378:metabolism* / Q000494:pharmacology
D003574:Cytochrome c Group; D013455:Sulfur; D000255:Adenosine Triphosphate; D010088:Oxidoreductases; D006864:Hydrogenase