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The chloroplast ATP synthase (CF1Fo) contains a specific feature to the green lineage a γ-subunit redox domain that contains a cysteine couple which interacts with the torque-transmitting βDELSEED-loop. This thiol modulation equips CF1Fo with an important environmental fine-tuning mechanism. In vitro, disulfide formation in the γ-redox domain slows down the activity of the CF1Fo at low transmembrane electrochemical proton gradient ( [Formula see text] ), which agrees with its proposed role as chock based on recently solved structure. Th
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