Johnson, Brittany J. Antholine, William E. Lindeman, Sergey V. Graham, Michael J. Mankad, Neal P. A One-Hole Cu<sub>4</sub>S Cluster with N<sub>2</sub>O Reductase Activity: A Structural and Functional Model for Cu<sub>Z</sub>* During bacterial denitrification, two-electron reduction of N<sub>2</sub>O occurs at a [Cu<sub>4</sub>(μ<sub>4</sub>-S)] catalytic site (Cu<sub>Z</sub>*) embedded within the nitrous oxide reductase (N<sub>2</sub>OR) enzyme. In this Communication, an amidinate-supported [Cu<sub>4</sub>(μ<sub>4</sub>-S)] model cluster in its one-hole (<i>S</i> = <sup>1</sup>/<sub>2</sub>) 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 [Cu<sub>4</sub>(μ<sub>4</sub>-S)] model complexes with catalytically relevant oxidation states for the first time. More importantly, N<sub>2</sub>O is reduced by the one-hole cluster to produce N<sub>2</sub> and the two-hole cluster, thereby completing a closed cycle for N<sub>2</sub>O reduction. Not only is the title complex thus the best structural model for Cu<sub>Z</sub>* to date, but it also serves as a functional Cu<sub>Z</sub>* mimic. cluster;two-electron redox series;two-hole redox partner;Cu Z;N 2 O Reductase Activity;N 2 O reduction;N 2 O;N 2;model;One-Hole Cu 4 S Cluster 2016-09-29
    https://acs.figshare.com/articles/dataset/A_One-Hole_Cu_sub_4_sub_S_Cluster_with_N_sub_2_sub_O_Reductase_Activity_A_Structural_and_Functional_Model_for_Cu_sub_Z_sub_/3976608
10.1021/jacs.6b05480.s002