Abstract
This chapter discusses the proton permeability of membrane sector (F 0 ) of H + -transporting ATP synthase (F 0 F 1 ) from a thermophilic bacterium. The membrane moiety of H + -transporting ATP synthase (F 0 F 1 ) that catalyzes ATP synthesis is the H + pathway across the membrane. This F 0 moiety can be easily prepared by treating F 0 F 1 with urea or a chaotropic anion and the resulting F 0 , when inlayed in phospholipid vesicles, shows H + conductivity; that is, protons are taken up when valinomycin is added to K + -loaded F 0 vesicles. The velocity of H + uptake is almost proportional to the amount of F 0 added. Stable preparations of TF 0 F 1 (H + -transporting ATP synthase from the thermophilic bacterium PS3) together with a simple procedure to prepare the H + -conducting TF 0 moiety result in an interesting system to study H + translocation through membrane proteins.
Published Version
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