Next Article in Journal
Antibacterial, Antifungal and Cytotoxic Activities of Two Flavonoids from Retama raetam Flowers
Next Article in Special Issue
IBS-Catalyzed Regioselective Oxidation of Phenols to 1,2-Quinones with Oxone®
Previous Article in Journal
Chemical Composition and Insecticidal Activity Against Sitophilus zeamais of the Essential Oils Derived from Artemisia giraldii and Artemisia subdigitata
Previous Article in Special Issue
Reaction of Iodonium Ylides of 1,3-Dicarbonyl Compounds with HF Reagents
Article Menu

Article Versions

Export Article

Open AccessReview
Molecules 2012, 17(6), 7266-7283; doi:10.3390/molecules17067266

Hypervalent Nonbonded Interactions of a Divalent Sulfur Atom. Implications in Protein Architecture and the Functions

Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka-shi, Kanagawa 259-1292, Japan
*
Author to whom correspondence should be addressed.
Received: 21 May 2012 / Revised: 6 June 2012 / Accepted: 8 June 2012 / Published: 13 June 2012
(This article belongs to the Special Issue Hypervalent Compounds)
Download PDF [482 KB, uploaded 18 June 2014]   |  

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., πO → σS* versus nO → σS* directionality). The difference was ascribed to the HOMO of the amide group, which expands in the vertical direction (πO) rather than in the plane (nO). S···X interactions in four model proteins, phospholipase A2 (PLA2), ribonuclease A (RNase A), insulin, and lysozyme, have also been analyzed. The results suggested that S···X interactions would be important factors that control not only the three-dimensional structure of proteins but also their functions to some extent. Thus, S···X interactions will be useful tools for protein engineering and the ligand design.
Keywords: Protein Data Bank; chalcogen bonds; σ-hole bonds; molecular assembly; protein engineering; drug design Protein Data Bank; chalcogen bonds; σ-hole bonds; molecular assembly; protein engineering; drug design
Figures

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Iwaoka, M.; Isozumi, N. Hypervalent Nonbonded Interactions of a Divalent Sulfur Atom. Implications in Protein Architecture and the Functions. Molecules 2012, 17, 7266-7283.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top