The a and b subunits constitute the stator elements in the F-o sector of F1
Fo-ATP synthase. Both subunits have been difficult to study by physical mea
ns, so most of the information on structure and function relationships in t
he a and b subunits has been obtained using mutagenesis in combination with
biochemical methods. These approaches were used to demonstrate that the a
subunit in association with the ring of c subunits houses the proton channe
l through F1Fo-ATP synthase. The map of the amino acids contributing to the
proton channel is probably complete. The two b subunits dimerize, forming
an extended flexible unit in the peripheral stalk Linking the F-1 and F-o s
ectors. The unique characteristics of specific amino acid substitutions aff
ecting the a and b subunits suggested differential effects on rotation duri
ng F1Fo-ATPase activity.