产气荚膜梭菌质子转运三磷酸腺苷酶的性质与功能
Properties and function of the proton-translocating adenosine triphosphatase of Clostridium perfringens.
作者信息
Hasan S M, Rosen B P
出版信息
J Bacteriol. 1979 Nov;140(2):745-7. doi: 10.1128/jb.140.2.745-747.1979.
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.
摘要
产气荚膜梭菌的生长受到能够消散或阻止电化学质子梯度形成的化合物的抑制。从该生物体制备的膜囊泡表现出对N，N'-二环己基碳二亚胺敏感的Mg2+依赖性腺苷三磷酸酶（ATP酶）活性。Mg2+-ATP酶活性在50℃时最佳，但未观察到明显的最适pH值。外翻膜囊泡对弱碱喹吖因荧光的ATP依赖性淬灭表明，Mg2+-ATP酶是一种能够产生电化学质子梯度的质子泵。外翻囊泡对Ca2+的ATP依赖性转运对Mg2+-ATP酶的解偶联剂和抑制剂敏感。
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