Abstract
The anion–π interaction is a well-recognized noncovalent force that is established between electron-deficient rings and anions. In the Communication by Antonio Frontera and co-workers on page 2708 ff., the relevance of this noncovalent interaction has been put on the scene by highlighting its critical role in the mechanism of sulfide:quinone oxidoreductase. In the first step of the enzymatic mechanism, an anionic intermediate is formed and is stabilized by an anion–π interaction that involves a cysteine residue and a flavin adenine dinucleotide (FAD) molecule. In the Cover picture, a dragon spits fireballs that represent the sulfur atoms of the two cysteine residues of the active site (disulfide bridge), of which one interacts with the FAD molecule placed on a branch.
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