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No Laughing Matter: The Unmaking of the Greenhouse Gas Dinitrogen Monoxide by Nitrous Oxide Reductase

  • Lisa K. Schneider
  • Anja Wüst
  • Anja Pomowski
  • Lin Zhang
  • Oliver Einsle
Part of the Metal Ions in Life Sciences book series (MILS, volume 14)

Abstract

The gas nitrous oxide (N2O) is generated in a variety of abiotic, biotic, and anthropogenic processes and it has recently been under scrutiny for its role as a greenhouse gas. A single enzyme, nitrous oxide reductase, is known to reduce N2O to uncritical N2, in a two-electron reduction process that is catalyzed at two unusual metal centers containing copper. Nitrous oxide reductase is a bacterial metalloprotein from the metabolic pathway of denitrification, and it forms a 130 kDa homodimer in which the two metal sites CuA and CuZ from opposing monomers are brought into close contact to form the active site of the enzyme. CuA is a binuclear, valence-delocalized cluster that accepts and transfers a single electron. The CuA site of nitrous oxide reductase is highly similar to that of respiratory heme-copper oxidases, but in the denitrification enzyme the site additionally undergoes a conformational change on a ligand that is suggested to function as a gate for electron transfer from an external donor protein. CuZ, the tetranuclear active center of nitrous oxide reductase, is isolated under mild and anoxic conditions as a unique [4Cu:2S] cluster. It is easily desulfurylated to yield a [4Cu:S] state termed CuZ * that is functionally distinct. The CuZ form of the cluster is catalytically active, while CuZ * is inactive as isolated in the [3Cu1+:1Cu2+] state. However, only CuZ * can be reduced to an all-cuprous state by sodium dithionite, yielding a form that shows higher activities than CuZ. As the possibility of a similar reductive activation in the periplasm is unconfirmed, the mechanism and the actual functional state of the enzyme remain under debate. Using enzyme from anoxic preparations with CuZ in the [4Cu:2S] state, N2O was shown to bind between the CuA and CuZ sites, suggesting direct electron transfer from CuA to the substrate after its activation by CuZ.

Keywords

copper enzymes global warming nitrogen cycle nitrous oxide X-ray crystallography 

Notes

Acknowledgment

The authors thank Peter Kroneck, Walter Zumft, Jörg Simon, Sofia Pauleta, and Isabel Moura for stimulating discussions. This work was supported by Deutsche Forschungsgemeinschaft, Deutscher Akademischer Austauschdienst, the BIOSS Centre for Biological Signalling Studies, and the European Research Council.

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© Springer Science+Business Media Dordrecht 2014

Authors and Affiliations

  • Lisa K. Schneider
    • 1
  • Anja Wüst
    • 1
  • Anja Pomowski
    • 1
  • Lin Zhang
    • 1
  • Oliver Einsle
    • 1
  1. 1.Institute for BiochemistryAlbert-Ludwigs-Universität FreiburgFreiburg im BreisgauGermany

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