The modeling of the hydrogenase active sites will be reviewed from a historical perspective, but emphasizing recent trends.  These active sites are unusual in biology because of their unusual ligands and unusual oxidation states for Fe and Ni.  Not only do these sites feature both cyanide and CO, they form hydrido complexes as intermediates in the interconversion of H+/H2.  Subsequent to the crystallographic and IR-spectroscopic of these enzymes, models have focused on carbonyl derivative of Fe and Ni thiolates.  Modern models, which are both structural and functional, incorporate hydride ligands and redox cofactors.

Modeling of hydrogenase active sites, an overview

246th National Meeting (2013)

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