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

Version 2 2024-03-12, 18:36
Version 1 2023-10-19, 16:31
journal contribution
posted on 2024-03-12, 18:36 authored by Souvik RoySouvik Roy, Sandip Shinde, G. Alexander Hamilton, Hilairy E. Hartnett, Anne K. Jones
<p>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 [(??SRS){Fe(CO)3}2] cluster on reaction with [Fe3(CO)12]. UV/Vis and FTIR spectroscopy demonstrate formation of the desired complex.</p>

History

School affiliated with

  • School of Chemistry (Research Outputs)

Publication Title

European Journal of Inorganic Chemistry

Volume

2011

Issue

7

Pages/Article Number

1050-1055

Publisher

Wiley

ISSN

1434-1948

Date Submitted

2020-04-16

Date Accepted

2010-08-17

Date of First Publication

2010-11-17

Date of Final Publication

2011-03-01

ePrints ID

40686