Significance The ATP synthases of many anaerobic archaea have an unusual motor subunit c that otherwise is only found in eukaryotic V1VO ATPases. The evolutionary switch from synthase to hydrolase… Click to show full abstract
Significance The ATP synthases of many anaerobic archaea have an unusual motor subunit c that otherwise is only found in eukaryotic V1VO 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.
               
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