Insights into Nitrous Oxide Reductase

Sofia R. Pauleta, Cíntia Carreira, Isabel Moura

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

10 Citations (Scopus)


Nitrous oxide reductase is the enzyme that catalyses the last step of the denitrification pathway, reducing nitrous oxide to dinitrogen gas. This enzyme is a functional homodimer with two copper centres, CuA and a "CuZ centre", located in different domains. The CuA centre is the electron transferring centre, while the catalytic centre is the "CuZ centre", a unique metal centre in biology - a tetranuclear copper centre with a μ4-bridging sulphide. The enzyme has been isolated with the "CuZ centre" in two different forms, CuZ(4Cu2S) and CuZ∗(4Cu1S), with the first presenting an additional μ2-sulphur atom as a bridging ligand between CuI and CuIV of the "CuZ centre", whereas the second form was identified as a water-derived molecule. Spectroscopic analysis of CuZ∗(4Cu1S), together with computational studies, indicated that there is a hydroxide bound to CuI. Genomic analysis has identified the presence of two different types of nitrous oxide reductase, the typical and "atypical", with a single member of the last group having been isolated to date, from Wolinella succinogenes. Thus, here the structure of the "typical" nitrous oxide reductase with either CuZ(4Cu2S) or CuZ∗(4Cu1S), as well as its spectroscopic and catalytic properties, will be discussed.

Original languageEnglish
Title of host publicationMetalloenzymes in Denitrification
Subtitle of host publicationApplications and Environmental Impacts
PublisherRoyal Society of Chemistry
Number of pages29
Publication statusPublished - Jan 2017

Publication series

NameRSC Metallobiology
ISSN (Print)2045547X


  • copper
  • nitrous oxide
  • nitrous oxide reductase


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