Hypervalent nonbonded interactions of a divalent sulfur atom. Implications in protein architecture and the functions.

ABSTRACT: In organic molecules a divalent sulfur atom sometimes adopts weak coordination to a proximate heteroatom (X). Such hypervalent nonbonded S···X interactions can control the molecular structure and chemical reactivity of organic molecules, as well as their assembly and packing in the solid state. In the last decade, similar hypervalent interactions have been demonstrated by statistical database analysis to be present in protein structures. In this review, weak interactions between a divalent sulfur atom and an oxygen or nitrogen atom in proteins are highlighted with several examples. S···O interactions in proteins showed obviously different structural features from those in organic molecules (i.e., π(o) → σ(s)* versus n(o) → σ(s)* directionality). The difference was ascribed to the HOMO of t

SUBMITTER: Iwaoka M 

PROVIDER: S-EPMC6269016 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature