ATP synthesis in an ancient ATP synthase at low driving forces

Abstract

Significance The ATP synthases of many anaerobic archaea have an unusual motor subunit c that otherwise is only found in eukaryotic V 1 V O ATPases. The evolutionary switch from synthase to hydrolase is thought to be caused by a doubling of the rotor subunit c , followed by a loss of the ion binding site. By purification and reconstitution of an ATP synthase with a V-type c subunit, we have unequivocally demonstrated, against expectations, the capability of such an enzyme to synthesize ATP at physiological relevant driving forces of 90 to 150 mV. This is the long-awaited answer to an eminent question in microbial energetics and physiology, especially for life near the thermodynamic limit of ATP synthesis.