Abstract
An energy ratchet mechanism is exploited for the synthesis of a molecule. In the presence of adenosine triphosphate (ATP), hydrazone-bond formation between an aldehyde and hydrazide is accelerated and the composition at thermodynamic equilibrium is shifted towards the hydrazone. Enzymatic hydrolysis of ATP installs a kinetically stable state at which hydrazone is present at a higher concentration compared to the composition at thermodynamic equilibrium in the presence of the degradation products of ATP. It is shown that the kinetic state has an enhanced catalytic activity in the hydrolysis of an RNA-model compound.
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