Structure and function of H + -ATPase

摘要: (1) Extensive studies on proton-translocating ATPase (H+-ATPase) revealed that H+-ATPase is an energy transforming device universally distributed in membranes of almost all kinds cells. (2) Crystallization the catalytic portion (F1) showed F1 a hexagonal molecule with central hole. The diameter about 90 A and its molecular weight 380,000. (3) Use thermophilic permits complete reconstitution from five subunits (α, β, γ, δ, e) demonstration gate function γδe-complex, β (supported by α γ), H+-translocating functions subunits. (4) Studies using purified thermostable F0 H+-channel H+-ATPase. direct measurement H+-flux through F0, sequencing DCCD-binding protein, isolation F1-binding protein are described. (5) subunit stoichiometry may be α3β3γδe. (6) Reconstitution stable H+-ATPase-liposomes ATP directly synthesized flow H+ driven electrochemical potential gradient translocated hydrolysis. This rules out for hypothetical components do not belong to H+-driven synthesis. roles conformation change other phenomena synthesis also discussed.