Artificial [FeFe]-Hydrogenase: On Resin Modification of an Amino Acid to Anchor a Hexacarbonyldiiron Cluster in a Peptide Framework

Roy, Souvik, Shinde, Sandip, Hamilton, G. Alexander, Hartnett, Hilairy E. and Jones, Anne K. (2011) Artificial [FeFe]-Hydrogenase: On Resin Modification of an Amino Acid to Anchor a Hexacarbonyldiiron Cluster in a Peptide Framework. European Journal of Inorganic Chemistry, 2011 (7). pp. 1050-1055. ISSN 1434-1948

Full content URL: https://doi.org/10.1002/ejic.201000979

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Item Type:Article
Item Status:Live Archive

Abstract

A general method for immobilization of synthetic analogues of the [FeFe]‐hydrogenase in designed peptides via on resin modification of an amino acid side chain with a dithiol functional group is described. Utilizing a unique amine side chain as anchor, the dithiol unit is coupled to the peptide via formation of an amide. This dithiol unit precisely positions the two required sulfur atoms for the formation of a [(μ‐SRS){Fe(CO)3}2] cluster on reaction with [Fe3(CO)12]. UV/Vis and FTIR spectroscopy demonstrate formation of the desired complex.

Keywords:Bioinorganic chemistry, Bioorganometallic chemistry, Enzyme models, Hydrogenase, Peptidomimetics, Designed peptide
Subjects:F Physical Sciences > F120 Inorganic Chemistry
C Biological Sciences > C720 Biological Chemistry
F Physical Sciences > F100 Chemistry
C Biological Sciences > C700 Molecular Biology, Biophysics and Biochemistry
F Physical Sciences > F161 Organometallic Chemistry
Divisions:College of Science > School of Chemistry
ID Code:40686
Deposited On:16 Apr 2020 15:37

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