PMID: 40963Nov 1, 1979

Properties and function of the proton-translocating adenosine triphosphatase of Clostridium perfringens

Journal of Bacteriology
S M Hasan, B P Rosen


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.


Feb 9, 2005·Microbiology·Fanqiang WangEva R Kashket

Related Concepts

Adenosine Triphosphatases
Phospholipid-translocating ATPase Activity
ATP12A gene
Uncouplers [MoA]
Clostridium perfringens
Proton Pump

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