The chloroplast adenosine triphosphate (ATP) synthase is located in the thy
lakoid membrane and synthesizes ATP from adenosine diphosphate and inorgani
c phosphate at the expense of the electrochemical proton gradient formed by
light-dependent electron flow. The structure, activities, and mechanism of
the chloroplast ATP synthase are discussed. Emphasis is given to the inher
ent structural asymmetry of the ATP synthase and to the implication of this
asymmetry to the mechanism of ATP synthesis and hydrolysis. A critical eva
luation of the evidence in support of and against the notion that one part
of the enzyme rotates with respect to other parts during catalytic turnover
is presented. It is concluded that although rotation can occur, whether it
is required for activity of the ATP synthase has not been established uneq
uivocally.