A One-Hole Cu₄S Cluster with N₂O Reductase Activity: A Structural and Functional Model for Cu_Z*

Abstract

During bacterial denitrification, two-electron reduction of N₂O occurs at a [Cu₄(μ₄-S)] catalytic site (Cu_Z*) embedded within the nitrous oxide reductase (N₂OR) enzyme. In this Communication, an amidinate-supported [Cu₄(μ₄-S)] model cluster in its one-hole (S = ¹/₂) redox state is thoroughly characterized. Along with its two-hole redox partner and fully reduced clusters reported previously, the new species completes the two-electron redox series of [Cu₄(μ₄-S)] model complexes with catalytically relevant oxidation states for the first time. More importantly, N₂O is reduced by the one-hole cluster to produce N₂ and the two-hole cluster, thereby completing a closed cycle for N₂O reduction. Not only is the title complex thus the best structural model for Cu_Z* to date, but it also serves as a functional Cu_Z* mimic.