Abstract
Synthetic metalloenzyme modeling studies are pursued to identify the essential ligation components of the transition metal in the active site. Most metalloenzyme active sites utilize an array of amino acids serving as the scaffold that stabilizes the metal binding site and assists in the catalytic action of the enzyme. Mono-[Fe] hydrogenase catalyzes the heterolytic cleavage of H2, and its structure has been shown to exhibit an array of non-amino acid ligands bound to the metal center. This unique metal center features three coordinated organic ligands: thiolato-SCys, pyridone-N, and acyl-C, all arranged in a facial triad on the Fe(II) octahedron. For synthetic modeling of the facial ligation of the mono-[Fe] hydrogenase active site, anthracene has been identified as a promising scaffold architecture on which the ligands may be deployed.
GRAPHICAL ABSTRACT
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Notes
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