Artificial [FeFe]-hydrogenase: On resin modification of an amino acid to anchor a hexacarbonyldiiron cluster in a peptide framework

Souvik Roy, Sandip Shinde, G. Alexander Hamilton, Hilairy E. Hartnett, Anne Katherine Jones

Research output: Contribution to journalArticle

33 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1050-1055
Number of pages6
JournalEuropean Journal of Inorganic Chemistry
Issue number7
DOIs
Publication statusPublished - Mar 2011

Fingerprint

Hydrogenase
Anchors
Resins
Amino Acids
Peptides
Carbon Monoxide
Sulfur
Amides
Functional groups
Amines
Spectroscopy
Atoms
dithiol

Keywords

  • Bioinorganic chemistry
  • Bioorganometallic chemistry
  • Designed peptide
  • Enzyme models
  • Hydrogenase
  • Peptidomimetics

ASJC Scopus subject areas

  • Inorganic Chemistry

Cite this

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.; Jones, Anne Katherine.

In: European Journal of Inorganic Chemistry, No. 7, 03.2011, p. 1050-1055.

Research output: Contribution to journalArticle

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