ECS-based investigation of chloroplast ATP synthase regulation

BioRxiv : the Preprint Server for Biology
Felix BuchertP. Joliot


The chloroplast ATP synthase (CF1Fo) contains a specific feature to the green lineage: a {gamma}-subunit redox domain which contains a cysteine couple and interacts with the torque-generating {beta}DELSEED-loop. Based on the recently solved structure of this domain, it was proposed to function as a chock. In vitro, {gamma}-disulfide formation slows down the activity of the CF1Fo at low transmembrane electrochemical proton gradient ({Delta}H+). Here, we utilize in vivo absorption spectroscopy measurements for functional CF1Fo activity characterization in Arabidopsis leaves. The spectroscopic method allows us to measure the {Delta}H+ present in dark-adapted leaves, and to identify its mitochondrial sources. Furthermore, we follow the fate of the extra {Delta}H+ generated by an illumination, including its osmotic and electric components, and from there we estimate the lifetime of the light-generated ATP. In contrast with a previous report [Joliot and Joliot, Biochim. Biophys. Acta, 1777 (2008) 676-683], the CF1Fo {gamma}-subunit exists mostly in an oxidized form in the dark-adapted state. To study the redox regulation of the CF1Fo, we used thiol agent infiltration in WT and a mutant that does not form the {gamma}-disulfide. The ob...Continue Reading

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