Swiss Policies for more Food Security

Resource-poor yet blissful Switzerland is also one of the most food-secure countries in the world: there are abundant food supplies, relatively low retail prices in terms of purchasing power parity, with few poverty traps. Domestic production covers 70% of net domestic consumption. A vast and efficient food reserve scheme insures against import disruptions. Nonetheless, the food security contribution by the four sectoral policies involved is mutually constrained: our agriculture is protected by the world’s highest tariffs. Huge subsidies, surface payments, and some production quotas substitute market signals with rent maximisation. Moreover, these inefficiencies also prevent trade and investment policies which would keep markets open, development policies which would provide African farmers with the tools to become more competitive, and supply policies which would work against speculators. The paralysing effect of Swiss agricultural policies is exacerbated by new “food security subsidies” in the name of “food sovereignty” while two pending people’s initiatives might yet increase the splendid isolation which in effect reduce Swiss farmer competitiveness and global food security. Is there a solution? Absent a successful conclusion of the Doha Round (WTO) or a Transatlantic Trade and Investment Partnership Agreement (TTIP) further market openings and a consequent “recoupling” of taxpayer support to public goods production remain highly un-likely. To the very minimum Switzerland should resume the agricultural reform process, join other countries trying to prevent predatory behaviour of its investors in developing countries, and regionalise its food reserve.

Mimicking respiratory phosphorylation using purified enzymes

The enzymes of oxidative phosphorylation are a striking example of the functional association of multiple enzyme complexes, working together to form ATP from cellular reducing equivalents. These complexes, such as cytochrome c oxidase or the ATP synthase, are typically investigated individually and therefore, their functional interplay is not well understood. Here, we present methodology that allows the co-reconstitution of purified terminal oxidases and ATP synthases in synthetic liposomes. The enzymes are functionally coupled via proton translocation where upon addition of reducing equivalents the oxidase creates and maintains a transmembrane electrochemical proton gradient that energizes the synthesis of ATP by the F1F0 ATP synthase. The method has been tested with the ATP synthases from Escherichia coli and spinach chloroplasts, and with the quinol and cytochrome c oxidases from E. coli and Rhodobacter sphaeroides, respectively. Unlike in experiments with the ATP synthase reconstituted alone, the setup allows in vitro ATP synthesis under steady state conditions, with rates up to 90 ATP×s(-1)×enzyme(-1). We have also used the novel system to study the phenomenon of "mild uncoupling" as observed in mitochondria upon addition of low concentrations of ionophores (e.g. FCCP, SF6847) and the recoupling effect of 6-ketocholestanol. While we could reproduce the described effects, our data with the in vitro system does not support the idea of a direct interaction between a mitochondrial protein and the uncoupling agents as proposed earlier.