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Artificial [FeFe]‐Hydrogenase: On Resin Modification of an Amino Acid to Anchor a Hexacarbonyldiiron Cluster in a Peptide Framework
Author(s) -
Roy Souvik,
Shinde Sandip,
Hamilton G. Alexander,
Hartnett Hilairy E.,
Jones Anne K.
Publication year - 2011
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201000979
Subject(s) - chemistry , dithiol , hydrogenase , amine gas treating , amide , side chain , cluster (spacecraft) , peptide , fourier transform infrared spectroscopy , amino acid , sulfur , combinatorial chemistry , polymer chemistry , infrared spectroscopy , hydrogen , organic chemistry , chemical engineering , biochemistry , computer science , engineering , programming language , polymer
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 [Fe 3 (CO) 12 ]. UV/Vis and FTIR spectroscopy demonstrate formation of the desired complex.