BIOC 2580 Lecture Notes - Lecture 18: Atp Synthase, Chemiosmosis, Protonation
Document Summary
Boyer suggested that the atp synthase active site cycles between a form that tightly binds atp and a form that releases atp. The active site, in a cyclic fashion is formed, torn apart and then re-formed to allow the continued synthesis of atp. Structural basis for rotational catalysis: each subunit of f1 can assume 3 different conformations. The subunit interacts asymmetrically with the 3 3 complex causing the three subunits to have different conformations, each associated with differences in their adp/atp binding site. At a given time one subunit is in the loose conformation, another in the tight conformation and the third in the open conformation. Each subunit is able to cycle between these 3 forms. During catalysis, the subunit rotates in the centre of the 3 3 complex. With each 1200 turn of the subunit a different face comes into contact with each subunit, rotating them between the three diff conformations.