title: Properties and function of the proton-translocating adenosine triphosphatase of Clostridium perfringens.
abstract: Growth of Clostridium perfringens was inhibited by compounds which dissipate or prevent the formation of electrochemical proton gradients. Membrane vesicles prepared from this organism exhibited Mg2+-dependent adenosine triphosphatase (ATPase) activity sensitive to N,N'-dicyclohexylcarbodiimide. Mg2+-ATPase activity was optimal of 50 degrees C, but no discrete pH optimum was observed. Adenosine triphosphate-dependent quenching of the fluorescence of the weak base quinacrine by everted membrane vesicles suggested that the Mg2+-ATPase is a proton pump capable of generating an electrochemical proton gradient. Adenosine triphosphate-dependent transport of Ca2+ by everted vesicles was sensitive to uncouplers and inhibitors of the Mg2+-ATPase.
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D003016:Clostridium perfringens / Q000201:enzymology*; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004563:Electrochemistry; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D013696:Temperature
chemical_list: D004024:Dicyclohexylcarbodiimide; D000251:Adenosine Triphosphatases; D008274:Magnesium; D002118:Calcium