Catalytic properties of β subunit isolated from chloroplast coupling factor 1.

The chloroplast coupling factor (CF1) was dissociated into subunits by the freezing-thawing procedure in the presence of 0.5 M NaBr and the β subunit was purified by ion-exchange chromatography on a DEAE-cellulose column. The β subunit did not catalyze ATP hydrolysis either in the presence or in the absence of reagents known to activate Mg(2+)-dependent ATPase activity of CF1. However, it manifested appreciable adenylate kinase-like and ATP-ADP γ-phosphate exchange activities. The adenylate kinase-like activity only slightly depended on Mg(2+) ions. Ethanol, and especially diadenosine pentaphosphate, inhibited the reaction effectively. In contrast, the ATP-ADP exchange activity was Mg(2+)-dependent. Ethanol and diadenosine pentaphosphate were poor inhibitors. Sulfite, the CF1-ATPase activator, and quercetin, its inhibitor, had a minor effect on catalytic activity of the β subunit.