This article reviews proton intake, charge transfer and proton release by F-ATPases, based in part on flash spectrophotometric studies on the chloroplast ATPase in thylakoid membranes, CF1Fo. The synthesis-coupled translocation of charges by CF1Fo (maximum rate <1500 s-1) and the dissipative flow through its exposed channel portion, CFo (rate >10 000 s-1), are extremely proton-specific (selectivity H+:K+>10(7):1). The proton-specific filter is located in CFo. Proton flow through exposed CFo can be throttled by adding subunit (&dgr;) or subunit &bgr; of CF1. These subunits thus may provide energy-transducing contacts between CF1 and CFo. Recently, we characterized two conditions where, in contrast to the above situation, proton intake by CF1Fo was decoupled from proton transfer across the main dielectric barrier: (a) CF1Fo structurally distorted by low ionic strength transiently trapped protons in a highly cooperative manner, but remained proton tight. This result has been interpreted in terms of Mitchell's proton well. (b) In the absence of nucleotides there is a proton slip. Addition of nucleotides (100 nmol l-1 ADP) abolished proton conduction but not proton intake by CF1Fo. These experiments functionally tag proton binding groups on CF1Fo that are located before the main dielectric barrier.

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