Maeda M, Kobayashi H, Futai M, Anraku Y
J Biochem. 1977 Jul;82(1):311-4. doi: 10.1093/oxfordjournals.jbchem.a131687.
The metabolic stabilities of bound adenine nucleotides in a membrane-bound ATPase (EF1) [EC 3.6.1.3] of Escherichia coli were studied by estimating their rates of turnover in vivo. Two-thirds of the bound ATP prelabelled with 32Pi in EF1 molecules was retained after 3 h in a chase medium. The bound ADP was chased rapidly with a half time of decrease of less than 1 h, the rate similar to that of cytoplasmic free nucleotides. These results suggest that bound ATP in the EF1 is not a direct intermediate in oxidative phosphorylation.
通过估计体内周转速率，研究了大肠杆菌膜结合ATP酶（EF1）[EC 3.6.1.3]中结合腺嘌呤核苷酸的代谢稳定性。在追踪培养基中培养3小时后，EF1分子中预先用32Pi标记的结合ATP的三分之二得以保留。结合的ADP被快速追踪，半衰期下降不到1小时，其速率与细胞质游离核苷酸的速率相似。这些结果表明，EF1中的结合ATP不是氧化磷酸化的直接中间体。
