Crystal Structures of [Fe]-Hydrogenase in Complex with Inhibitory Isocyanides: Implications for the H2-Activation Site.

The article presents a study which examines the implication of the crystal structures of iron (Fe)-hydrogenase for the activation site of H₂. The study involves several methods including the purification of Fe-hydrogenase from Methanothermobacter marburgensis, crystallization of protein-isocyanide complexes, and X-ray diffraction. The study reveals that the mode of isocyanide-binding to Fe-dehydrogenase shows that H₂ is bound to the iron site trans to the acyl ligand.