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 Hartnett; Anne Jones

doi:10.1002/ejic.201000979

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 Hartnett, Anne Jones

Research output: Contribution to journal › Article › peer-review

41 Scopus citations

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 language	English (US)
Pages (from-to)	1050-1055
Number of pages	6
Journal	European Journal of Inorganic Chemistry
Issue number	7
DOIs	https://doi.org/10.1002/ejic.201000979
State	Published - Mar 2011

Keywords

Bioinorganic chemistry
Bioorganometallic chemistry
Designed peptide
Enzyme models
Hydrogenase
Peptidomimetics

ASJC Scopus subject areas

Inorganic Chemistry

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10.1002/ejic.201000979

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

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, Designed peptide, Enzyme models, Hydrogenase, Peptidomimetics",

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T2 - On resin modification of an amino acid to anchor a hexacarbonyldiiron cluster in a peptide framework

AU - Roy, Souvik

AU - Shinde, Sandip

AU - Hamilton, G. Alexander

AU - Hartnett, Hilairy

AU - Jones, Anne

PY - 2011/3

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AB - 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.

KW - Bioinorganic chemistry

KW - Bioorganometallic chemistry

KW - Designed peptide

KW - Enzyme models

KW - Hydrogenase

KW - Peptidomimetics

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

Abstract

Keywords

ASJC Scopus subject areas

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