A 1-hole Cu4S cluster with N2O reductase activity: a structural and functional model for CuZ

• Published in: Journal of the American Chemical Society Vol. 138; no. 40; pp. 13107 - 13110
• Main Authors: Johnson, Brittany J., Antholine, William E., Lindeman, Sergey V., Graham, Michael J., Mankad, Neal P.
• Format: Journal Article
• Language: English
• Published: 03.10.2016
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/jacs.6b05480

During bacterial denitrification, two-electron reduction of N 2 O occurs at a [Cu 4 (μ 4 -S)] catalytic site (Cu Z *) embedded within the nitrous oxide reductase (N 2 OR) enzyme. In this communication, an amidinate-supported [Cu 4 (μ 4 -S)] model cluster in its 1-hole (S = ½) redox state is thoroughly characterized. Along with its 2-hole redox partner and fully reduced clusters reported previously, the new species completes the two-electron redox series of [Cu 4 (μ 4 -S)] model complexes with catalytically relevant oxidation states for the first time. More importantly, N 2 O is reduced by the 1-hole cluster to produce N 2 and the 2-hole cluster, thereby completing a closed cycle for N 2 O reduction. The title complex is thus not only the best structural model for Cu Z * to date, but it also serves as a functional Cu Z * mimic.