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Significance F-ATP synthase is a fundamental enzyme supplying adenosine triphosphate (ATP), spreading across all kingdoms of life. Despite remarkable conservation of its basic structure and function, biophysical studies have revealed discrete differences in the rotary mechanisms of bacterial and eukaryotic F1 -ATPases (the catalytic portions of the enzymes). Here, we analyzed the rotational dynamics ofParacoccus denitrificans F1 (PdF1 ), a bacterial F1 -ATPase that exhibits high homology with the core functional subunits of its mitochondrial counterpart. Notably, PdF1 possesses a simplified chemomechanical scheme different from that of all other F1 -ATPases. Our results reveal an unexpected diversity in the chemomechanical coupling cycle of the F1 -ATPase machinery and show that features such as homology or phylogenetic relationship cannot uniquely define the rotary scheme pattern.

proceedings of the national academy of sciences of the united states of america

The 3 × 120° rotary mechanism of Paracoccus denitrificans F 1 -ATPase is different from that of the bacterial and mitochondrial F 1 -ATPases