A mutation in human ATPase 6, which corresponds to E. coli subunit a, from leucine to arginine at position 156 may allow the movement of protons across the membrane, but not the rotation of the ring of c subunits. How might this possible mechanism affect the function of ATP synthase

H+ protons will not be delivered from the cytoplasm towards the extracellular side of the cell membrane

Explanation:

ATP synthases are enzymes that catalyze the hydrolysis of phosphate bonds in the adenosine triphosphate (ATP) or the formation of ATP from adenosine diphosphate (ADP) and phosphate. The hydrolysis of ATP produces the rotation of a ring composed of six or more structurally different ATPase C subunits. The rotation of this ring enables the delivery of H+ protons towards the extracellular membrane surface and this gradient is used to generate energy by producing ATP. In consequence, when the ATPase ring can not move, H+ will accumulate in the cytoplasm, the proton gradient through the membrane will not occur, and ATP will not be produced.