Cover Picture: On the Importance of Anion–π Interactions in the Mechanism of Sulfide:Quinone Oxidoreductase (Chem. Asian J. 11/2013) | Zendy

Bauzá Antonio | Zendy; Quiñonero David | Zendy; Deyà Pere M. | Zendy; Frontera Antonio | Zendy

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Cover Picture: On the Importance of Anion–π Interactions in the Mechanism of Sulfide:Quinone Oxidoreductase (Chem. Asian J. 11/2013)

Author(s) -

Bauzá Antonio,

Quiñonero David,

Deyà Pere M.,

Frontera Antonio

Publication year - 2013

Publication title -

chemistry – an asian journal

Language(s) - English

Resource type - Reports

SCImago Journal Rank - 1.18

H-Index - 106

eISSN - 1861-471X

pISSN - 1861-4728

DOI - 10.1002/asia.201390038

Subject(s) - chemistry , oxidoreductase , cysteine , flavin group , quinone , non covalent interactions , molecule , stereochemistry , sulfur , sulfide , photochemistry , hydrogen bond , enzyme , biochemistry , organic chemistry

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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