Details

Autor(en) / Beteiligte

• de Hatten, Xavier
• Bothe, Eberhardt
• Merz, Klaus
• Huc, Ivan
• Metzler-Nolte, Nils

Titel

A Ferrocene-Peptide Conjugate as a Hydrogenase Model System

Ist Teil von

• European Journal of Inorganic Chemistry, 2008-10, Vol.2008 (29), p.4530-4537

Ort / Verlag

Weinheim: WILEY-VCH Verlag

Erscheinungsjahr

2008

Link zum Volltext

Quelle

Wiley Blackwell Single Titles

Beschreibungen/Notizen

• 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 Mössbauer 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) A peptidic cysteine‐based macrocyclicligand with a ferrocene backbone is introduced, which combines key features of the natural enzyme in a hydrogenase mimic, namely an electro‐active group in spatial proximity to a diiron active‐site mimic, and coordination of this active‐site mimic to naturally occurring cysteine ligands.