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Control of chloroplast ATP synthase (CF0CF1) activity by Δ pH

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Abstract

A biphasic decay of the thiol modulated ATPase activity is observed at fast deenergization of the thylakoids achieved by turning off the light and simultaneous injection of the uncoupler nigericin. Most likely the rapid phase (τ1/2 = 5 s) represents an unstable, active Ef-form of the enzyme which decays to a less active, but more stable Es-form. The two forms have different substrate affinities. Deactivation and reactivation kinetics indicate that the transition from the Ef- to the Es-form is reversible, requires a low proton gradient (1 to 2 ΔpH units) and most probably involves the release and binding, respectively, of two protons from the thylakoid lumen phase to sites which have an apparent pK of 6.6. The Es-form decays to the inactive Ei-form with a half time of 90 s. Reactivation of the completely deactivated enzyme is a two-stage process comprising protonation of sites with a pK of 6.8 followed by protonation of sites of pK 4.9. The intermediate Es'-form has a decay time which is similar to that of the Es-form, but a different Km for ATP. Therefore we conclude that activation is not the exact reversal of deactivation. The results are discussed in terms of a model of ΔμH+-linked activation/deactivation.

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  1. Institut für Biochemie der Pflanzen, Heinrich-Heine-Universität Düsseldorf, D-40225, Düsseldorf, Germany

    Oliver Schwarz & Heinrich Strotmann

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  1. Oliver Schwarz
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  2. Heinrich Strotmann
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Schwarz, O., Strotmann, H. Control of chloroplast ATP synthase (CF0CF1) activity by Δ pH. Photosynthesis Research 57, 287–295 (1998). https://doi.org/10.1023/A:1006006907945

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