Mercury binding by ferrocenoyl peptides with sulfur-containing side chains: Electrochemical, spectroscopic and structural studies

Scully, Conor C. G., Jensen, Paul and Rutledge, Peter J. (2008) Mercury binding by ferrocenoyl peptides with sulfur-containing side chains: Electrochemical, spectroscopic and structural studies. Journal of Organometallic Chemistry, 693 17: 2869-2876. doi:10.1016/j.jorganchem.2008.06.005


Author Scully, Conor C. G.
Jensen, Paul
Rutledge, Peter J.
Title Mercury binding by ferrocenoyl peptides with sulfur-containing side chains: Electrochemical, spectroscopic and structural studies
Journal name Journal of Organometallic Chemistry   Check publisher's open access policy
ISSN 0022-328X
1872-8561
Publication date 2008-08-15
Sub-type Article (original research)
DOI 10.1016/j.jorganchem.2008.06.005
Volume 693
Issue 17
Start page 2869
End page 2876
Total pages 8
Editor G. Bertrand
R. D. Adams
W. A. Herrmann
Place of publication Lausanne, Switzerland
Publisher Elsevier
Language eng
Subject 0399 Other Chemical Sciences
Abstract Ferrocenoyl peptides incorporating amino acids derived from either l-methionine, l-cysteine or dl-homocysteine have been synthesised and investigated as agents for heavy metal binding and detection. Heavy metal–peptide interactions have been characterised using cyclic voltammetry to follow changes in the potential of the Fe(II)/Fe(III) redox couple, revealing that these systems interact with mercury(II) ions more strongly than with other thiophilic heavy metals such as cadmium(II), silver(I) and lead(II). Proton NMR experiments have demonstrated 1:1 peptide:mercury binding and enabled quantitative characterisation of this binding interaction. Crystal structures for two of these ferrocenoyl peptide derivatives have been elucidated, revealing that these compounds adopt a P-1,3′ open solid state conformation in the absence of mercury; this arrangement precludes intramolecular hydrogen bonding between chains, while extensive intermolecular hydrogen bonding is evident. The particular affinity of these systems for mercury(II) opens the possibility of incorporating them in new, biologically inspired sensors for detecting this toxic pollutant.
Formatted abstract


Keyword Bioorganometallic chemistry
Ferrocene compounds
Mercury
Toxic metal ions
Amino acids
Peptides
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Created: Fri, 29 Jan 2010, 00:28:08 EST by June Temby on behalf of Institute for Molecular Bioscience