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A One-Hole Cu4S Cluster with N2O Reductase Activity: A Structural and Functional Model for CuZ
Brittany J Johnson1, William E Antholine2, Sergey V Lindeman3
1Department of Chemistry, University of Illinois at Chicago , 845 West Taylor Street, Chicago, Illinois 60607, United States.
Journal of the American Chemical Society
|September 30, 2016
Summary
Researchers developed a novel copper-sulfur cluster model that mimics the nitrous oxide reductase (N2OR) enzyme
Area of Science:
- Bioinorganic Chemistry
- Catalysis
- Environmental Science
Background:
- Bacterial denitrification involves the reduction of nitrous oxide (N2O) via the nitrous oxide reductase (N2OR) enzyme.
- The catalytic site of N2OR, known as CuZ*, contains a [Cu4(μ4-S)] cluster crucial for N2O reduction.
Purpose of the Study:
- To synthesize and characterize a novel amidinate-supported [Cu4(μ4-S)] model cluster in its one-hole redox state.
- To establish a complete two-electron redox series of [Cu4(μ4-S)] model complexes with catalytically relevant oxidation states.
- To demonstrate the functional mimicry of the CuZ* active site for N2O reduction.
Main Methods:
- Synthesis of an amidinate-supported [Cu4(μ4-S)] cluster.
- Electrochemical characterization of the cluster in its one-hole redox state.
- Spectroscopic analysis to confirm the cluster's structure and redox properties.
Main Results:
- The one-hole [Cu4(μ4-S)] cluster was thoroughly characterized.
- This cluster, along with its redox partners, completes the two-electron redox series of relevant [Cu4(μ4-S)] model complexes.
- The one-hole cluster successfully reduced N2O to N2, forming the two-hole cluster and completing a closed catalytic cycle.
Conclusions:
- The synthesized amidinate-supported [Cu4(μ4-S)] cluster is the best structural model for the CuZ* active site to date.
- This model complex functions as an effective mimic of the CuZ* enzyme, facilitating N2O reduction.
- The study provides crucial insights into the mechanism of N2O reduction in bacterial denitrification.
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