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Why do prime ministers or presidents appoint non‐elected experts, also known as technocrats, during economic crises? Do they appoint them for their expertise or for their commitment to pro‐market reforms? Answering this question is crucial for understanding and predicting the longer‐term role of technocrats in democracies. With the aid of unique data on the political and personal background of finance ministers in 13 parliamentary and semi‐presidential European democracies this article shows that commitment, not expertise is the primary driver of technocratic appointments during major economic crises. Technocrats are preferred over experienced politicians when the latter lack commitment to policy reform. An important implication of the findings is that technocratic appointments to top economic portfolios in West European countries are unlikely to become the norm outside economic crises, assuming economic crises are short‐lived and not recurring.

Quantum mechanical optimizations of theoretical enzymes (theozymes), which are predicted catalytic arrays of biological functionalities stabilizing a transition state, have been carried out for a set of nine diverse enzyme active sites. For each enzyme, the theozyme for the rate-determining transition state plus the catalytic groups modeled by side-chain mimics was optimized using B3LYP/6–31G(d) or, in one case, HF/3–21G(d) quantum mechanical calculations. To determine if the theozyme can reproduce the natural evolutionary catalytic geometry, the positions of optimized catalytic atoms, i.e., covalent, partial covalent, or stabilizing interactions with transition state atoms, are compared to the positions of the atoms in the X-ray crystal structure with a bound inhibitor. These structure comparisons are contrasted to computed substrate–active site structures surrounded by the same theozyme residues. The theozyme/transition structure is shown to predict geometries of active sites with an average RMSD of 0.64 Å from the crystal structure, while the RMSD for the bound intermediate complexes are significantly higher at 1.42 Å. The implications for computational enzyme design are discussed.