A Ferrocene–Peptide Conjugate as a Hydrogenase Model System

Autor: Ivan Huc, Nils Metzler-Nolte, Klaus Merz, Eberhardt Bothe, Xavier de Hatten
Rok vydání: 2008
Předmět:
Zdroj: European Journal of Inorganic Chemistry. 2008:4530-4537
ISSN: 1099-0682
1434-1948
DOI: 10.1002/ejic.200800566
Popis: This work introduces a bis(cysteine) ligand to build a small peptidic model system of hydrogenase enzymes. Fe(C5H4CO–Cys–OMe)2 (LH2) has been employed as a chelate for an iron–carbonyl complex, which mimics two essential structural properties of the hydrogenase class of enzymes, namely the coordination of the iron–carbonyl core to peptide ligands and the presence of an electrochemical relay in spatial proximity. The treatment of LH2 with Fe3(CO)12 yields LFe2(CO)6 (3a), which is the first peptide-coordinated iron hydrogenase active-site model complex. Compound 3a was fully characterized spectroscopically (1H NMR, 13C NMR, IR and Mossbauer spectroscopy, mass spectrometry and elemental analysis). A single-crystal X-ray analysis confirms the proposed structure and reveals a staggered conformation of the Fe2(CO)6S2 core. Fourier transform infrared (FTIR) spectroelectrochemistry reveals an electronic interaction between the peptide backbone and the iron–carbonyl cluster, but not with the ferrocene subsite. The introduction of this peptidic cysteine-based ligand into hydrogenase model chemistry helps to confirm the proposed cofactor biosynthesis and understand the electronic interplay between the metal–carbonyl active site and the protein environment in this important class of enzymes.(© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008)
Databáze: OpenAIRE
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