ATP synthesis in Halobacterium saccharovorum:  evidence that synthesis may be catalysed by an F0F1-ATP synthase.
Halobacterium saccharovorum synthesized ATP in response to a pH shift from 8 to 6.2.  Synthesis was inhibited by carbonyl cyanide m-chloro-phenylhydrazone, dicyclohexylcarbodiimide, and azide.  Nitrate, an inhibitor of the membrane-bound ATPase previously isolated from this organism, did not inhibit ATP synthesis.  N-Ethymaleimide, which also inhibited this ATPase, stimulated the production of ATP.  These observations suggested that H. saccharovorum synthesized and hydrolysed ATP using different enzymes and that the vacuolar-like ATPase activity previously described in H. saccharovorum was an ATPase whose function is yet to be identified.
Hochstein
L I
LI
Planetary Biology Branch, Ames Research Center, Moffett Field, California.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000096:biosynthesis* / Q000378:metabolism; D001386:Azides / Q000494:pharmacology; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D005033:Ethylmaleimide / Q000494:pharmacology; D006217:Halobacterium / Q000201:enzymology* / Q000378:metabolism / Q000502:physiology; D006863:Hydrogen-Ion Concentration; D009566:Nitrates / Q000494:pharmacology; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism / Q000502:physiology*
D001386:Azides; D009566:Nitrates; D004024:Dicyclohexylcarbodiimide; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases; D005033:Ethylmaleimide