Membrane-associated, energy-linked reactions in Bdellovibrio bacteriovorus.
Disrupted cells of Bdellovibrio bacteriovorus exhibited adenosine triphosphatase activity, 60 to 80% of which was in the soluble fraction. Dicyclohexylcarbodiimide did not inhibit the adenosine triphosphatase activity in membrane particles. The particles did not show energy-linked transhydrogenase activity. The activity of non-energy-linked transhydrogenase as well as the rate of oxygen consumption were higher in membrane particles of the host-independent strain than in the host-dependent strains. The uptake of amino acid uptake was inhibited by cyanide and by carbonyl cyanide p-trifluoromethoxyphenyl hydrazone. Valinomycin, in the presence of K+, did not inhibit the uptake, and only partial inhibition was exerted by arsenate and dicyclohexylarbodiimide. Sulfhydryl reagents inhibited amino acid uptake.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism*; D001419:Bacteria / Q000378:metabolism* / Q000648:ultrastructure; D001693:Biological Transport, Active / Q000187:drug effects; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D003486:Cyanides / Q000494:pharmacology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004734:Energy Metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism*; D014475:Uncoupling Agents / Q000494:pharmacology
D000596:Amino Acids; D003486:Cyanides; D010710:Phosphates; D014475:Uncoupling Agents; D004024:Dicyclohexylcarbodiimide; D009247:NADH, NADPH Oxidoreductases; D000251:Adenosine Triphosphatases