Energy coupling to nitrite respiration in the sulfate-reducing bacterium Desulfovibrio gigas.
By use of a membrane fraction prepared from Desulfovibrio gigas grown in a lactate-sulfate medium, synthesis of ATP was demonstrated to be coupled to the oxidation of molecular hydrogen and reduction of either nitrite or hydroxylamine. This phosphorylation was uncoupled from electron transport by pentachlorophenol, methyl viologen, and gramicidin, but not by oligomycin. The extrusion of protons from the cells was shown to be coupled to the hydrogen-nitrite respiratory system, and, assuming the localization of nitrite reductase on the outer side of the plasma membrane, H+/2e- values of 2.0 +/- 0.3 were obtained. Energy coupling observed with this system appears to be due to electron transfer-coupled proton translocation rather than vectorial electron transfer associated with hydrogen oxidation.
D000255:Adenosine Triphosphate / Q000096:biosynthesis*; D003901:Desulfovibrio / Q000378:metabolism*; D004579:Electron Transport; D006859:Hydrogen / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000378:metabolism; D009573:Nitrites / Q000378:metabolism*; D010084:Oxidation-Reduction; D014475:Uncoupling Agents / Q000494:pharmacology
D006898:Hydroxylamines; D009573:Nitrites; D014475:Uncoupling Agents; D019811:Hydroxylamine; D006859:Hydrogen; D000255:Adenosine Triphosphate