Decker S J, Lang D R
J Bacteriol. 1977 Jul;131(1):98-104. doi: 10.1128/jb.131.1.98-104.1977.
An adenosine triphosphatase (ATPase) mutant of Bacillus megaterium was isolated and characterized. This mutant (designated A37) was unable to grow on nonfermentable carbon sources and possessed less than 5% of the wild-type ATPase activity. Oxygen uptake by the mutant was comparable to that in the wild type. Sporulation in the wild type occurred in both glucose- and nitrogen-limiting media; however, A37 sporulated only in the nitrogen-limiting medium. The inability of A37 to sporulate in glucose-limiting medium seemed to be due to insufficient adenosine 5'-triphosphate (ATP) levels during the sporulation stages. Fructose, which can generate ATP via substrate-level phosphorylation, is equally efficient in stimulating ATP synthesis in the wild type and A37. Malate-stimulated ATP synthesis in the wild type was shown to have many characteristics associated with oxidative phosphorylation and was absent in the mutant. These data suggest that the ATPase deficiency results in the loss of oxidative phosphorylation.
分离并鉴定了巨大芽孢杆菌的一种三磷酸腺苷酶（ATP酶）突变体。该突变体（命名为A37）无法在非发酵性碳源上生长，其ATP酶活性不到野生型的5%。该突变体的氧气摄取与野生型相当。野生型在葡萄糖和氮限制培养基中均能形成芽孢；然而，A37仅在氮限制培养基中形成芽孢。A37在葡萄糖限制培养基中无法形成芽孢似乎是由于芽孢形成阶段三磷酸腺苷（ATP）水平不足。果糖可通过底物水平磷酸化产生ATP，在刺激野生型和A37的ATP合成方面同样有效。野生型中苹果酸刺激的ATP合成具有许多与氧化磷酸化相关的特征，而在突变体中则不存在。这些数据表明，ATP酶缺陷导致氧化磷酸化丧失。
