The most commonly quoted mechanism of the coupling between the electrochemi
cal proton gradient and the formation of ATP from ADP and P-i assumes that
all states of the FI portion of the ATP synthase have beta subunits in "tig
ht," " loose," and "open" conformations. Models based on this assumption ar
e inconsistent with some of the available experimental evidence. A mechanis
m that includes an additional beta subunit conformation, "closed," observed
in the rat liver structure overcomes these difficulties.