A One-Hole Cu4S Cluster with N2O Reductase Activity: A Structural and Functional Model for CuZ
Document Type
Article
Language
eng
Format of Original
4 p.
Publication Date
2016
Publisher
American Chemical Society
Source Publication
Journal of the American Chemical Society
Source ISSN
0002-7863
Original Item ID
DOI: 10.1021/jacs.6b05480
Abstract
During bacterial denitrification, two-electron reduction of N2O occurs at a [Cu4(μ4-S)] catalytic site (CuZ*) 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 CuZ* to date, but it also serves as a functional CuZ* mimic.
Recommended Citation
Johnson, Brittany J.; Antholine, William E.; Lindeman, Sergey; Graham, Michael J.; and Mankad, Neal P., "A One-Hole Cu4S Cluster with N2O Reductase Activity: A Structural and Functional Model for CuZ" (2016). Chemistry Faculty Research and Publications. 528.
https://epublications.marquette.edu/chem_fac/528
Comments
Accepted version. Journal of the American Chemical Society, Vol. 138, No. 40 (2016): 13107-13110. DOI. © 2016 American Chemical Society. Used with permission.