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Peer-reviewedCC BYInorganic chemistry

Tetranuclear Copper Cluster of N2O Reductase: A Distinctive Copper-Sulfur Metallocluster.

  • Sofia R Pauleta1,2
  • José J G Moura3
  • Isabel Moura3
  1. 1Microbial Stress Lab, UCIBIO - Applied Molecular Biosciences Unit, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, 2829-516Caparica, Portugal.
  2. 2Associate Laboratory i4HB - Institute for Health and Bioeconomy, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, 2829-516Caparica, Portugal.
  3. 3LAQV, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, 2829-516Caparica, Portugal.
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Abstract

Copper is an essential element involved in several cofactors and organometallic compounds used as catalysts. Although most biological copper centers contain one to three copper ions, nature has evolved a unique tetranuclear copper-sulfur cluster that has attracted the attention of both biochemists and inorganic chemists. This multinuclear copper center has only been observed in one enzyme, nitrous oxide reductase, which catalyzes the reduction of nitrous oxide to dinitrogen, the final step of the denitrification pathway. The structural, spectroscopic, and kinetic properties of this [4CuS] cluster have been the subject of extensive investigation, revealing that it exists in two distinct forms within the enzyme, CuZ[4Cu:2S] and CuZ*[4Cu:1S], with different oxidation states, spectroscopic signatures, and catalytic properties. These features are discussed together with recent advances in understanding the biosynthesis and assembly of this cluster. Inorganic chemists have synthesized a variety of structural and functional models of the CuZ cluster, although none fully reproduces the electronic structure and catalytic efficiency of the native active center. This review discusses the interplay between biological and synthetic studies, illustrating how advances in one field continue to inspire progress in the other while identifying the challenges that must be overcome to achieve truly functional biomimetic catalysts.

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Cite

BibTeXRIS
BibTeX
@article{pauleta2026tetranuclear,
  title = {{Tetranuclear Copper Cluster of N2O Reductase: A Distinctive Copper-Sulfur Metallocluster.}},
  author = {Sofia R Pauleta and José J G Moura and Isabel Moura},
  journal = {Inorganic chemistry},
  year = {2026},
  month = oct,
  doi = {10.1021/acs.inorgchem.6c04238},
  url = {https://europepmc.org/article/MED/42895402},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Tetranuclear Copper Cluster of N2O Reductase: A Distinctive Copper-Sulfur Metallocluster.
AU  - Sofia R Pauleta
AU  - José J G Moura
AU  - Isabel Moura
PY  - 2026
DA  - 2026/10/01
JO  - Inorganic chemistry
DO  - 10.1021/acs.inorgchem.6c04238
UR  - https://europepmc.org/article/MED/42895402
AB  - Copper is an essential element involved in several cofactors and organometallic compounds used as catalysts. Although most biological copper centers contain one to three copper ions, nature has evolved a unique tetranuclear copper-sulfur cluster that has attracted the attention of both biochemists and inorganic chemists. This multinuclear copper center has only been observed in one enzyme, nitrous oxide reductase, which catalyzes the reduction of nitrous oxide to dinitrogen, the final step of the denitrification pathway. The structural, spectroscopic, and kinetic properties of this [4CuS] cluster have been the subject of extensive investigation, revealing that it exists in two distinct forms within the enzyme, CuZ[4Cu:2S] and CuZ*[4Cu:1S], with different oxidation states, spectroscopic signatures, and catalytic properties. These features are discussed together with recent advances in understanding the biosynthesis and assembly of this cluster. Inorganic chemists have synthesized a variety of structural and functional models of the CuZ cluster, although none fully reproduces the electronic structure and catalytic efficiency of the native active center. This review discusses the interplay between biological and synthetic studies, illustrating how advances in one field continue to inspire progress in the other while identifying the challenges that must be overcome to achieve truly functional biomimetic catalysts.
SN  - 0020-1669
SN  - 1520-510X
ER  -