In the ecological nitrogen cycle, an enzyme called nitrous oxide reductase converts N2O into completely benign materials such as N2 and H2O. The N2O activating site in this particular enzyme is a Cu4S cluster, known as Cuz*.Although nitrous oxide reductase has been the focus of several structural studies, very little is known about the different binding modes of N2O, its activation and the catalytic reduction mechanism. We report the synthesis and characterization of two new copper monosulfide clusters structurally related to Cuz* and we anticipate that kinetic destabilization from hydrogen bond donors within the secondary coordination or thermodynamic destabilization from electron-releasing phosphine ligands will show increased reactivity with N2O.

Synthetic model complexes structurally related to the Cu<sub>z</sub>* site of nitrous oxide reductase

248th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Synthetic model complexes structurally related to the Cuz* site of nitrous oxide reductase

Synthetic model complexes structurally related to the Cu_z* site of nitrous oxide reductase