Chemiosmosis

T state

shape of the enzymatic portion that clamps down on the products ATP + H2O

aspartic acid

status of the protonatable aminoacyl of the merry-go-round protein on 8 of ten subunits that are in rotating contact with the inner membrane phospholipids

c subunit

ten of these form a merry-go-round of rotating proteins within the mitochondrial inner membrane of ATP synthase

arginine

aminoacyl of the stationary inner membrane subunit that attracts the next merry-go-round subunit forward to rotate the complex

glutamate

aminoacyl of the enzymatic portion of ATP synthase that forms the "water trap" by binding to the hydrogens of that product

O-state

denatured shape of the enzymatic portion caused by the rotating "cam shaft" disrupting its parallel beta sheet to release ATP and H2O to the matrix

L state

shape of the enzymatic portion bound to ADP + Pi

aspartate

status of the protonatable aminoacyl of the merry-go-round protein upon first contact with half-channel of the stationary integral membrane subunit

lysine

aminoacyl of the enzymatic portion of ATP synthase that forms the "water trap" by binding to the oxygen of that product

a subunit

inner membrane protein of ATP synthase that is stationary relative to a rotating merry-go-round, with two half-channels for delivering protons to the matrix from the merry-go-round subunit at first contact, and replacing that proton from an adjacent half channel from the intermembrane space

gamma subunit

asymmetric "cam shaft" that is rotated to induce shape changes on the enzymatic portions of ATP synthase

alpha/beta subunit dimer

catalytic portion of the ATP synthase complex that projects into the matrix where it undergoes three different shape changes