Studies on the turnovers in vivo of adenosine di- and triphosphates in a coupling factor of Escherichia coli.
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.
D000244:Adenosine Diphosphate / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D010086:Oxidative Phosphorylation Coupling Factors / Q000378:metabolism*; D010101:Oxygen Consumption; D010710:Phosphates / Q000378:metabolism
D010086:Oxidative Phosphorylation Coupling Factors; D010710:Phosphates; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases