Mono-[Fe] Hydrogenase catalyzes the heterolytic splitting of dihydrogen (H2), utilizing H2 as a hydride source for one step in the methanogenic, nickel-independent reduction of carbon dioxide (CO2) to methane (CH4). The active site Fe is ligated by a unique array of ligands: an non-peptide organometallic Fe-C(O) acyl unit; a non-peptide pyridone-N; a cysteine thiolate; as well as two CO and one solvent binding site. In our synthetic modeling studies, we have constructed bi-, tri- and tetra-dentate ligands (NS, CNS, NNS, CNNS) containing all or some of these features. Isolated crystal structures and reactivity have shed light on the biogenesis and reactivity of the active site. In all cases, both the acyl and deprotonated pyridone units increase stability of the bound CO ligands at room temperature. Synthetic strategies to manage the dinucleating propensity of the pyridone and thiolate moieties will be discussed.

Synthetic modeling of mono-[Fe] hydrogenase: Role of Fe-acyl and pyridone donors

248th National Meeting (2014)

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