Insights into Nitrous Oxide Reductase

Sofia R. Pauleta, Cíntia Carreira, Isabel Moura

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Citations (Scopus)

Abstract

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
Pages141-169
Number of pages29
Volume7
DOIs
Publication statusPublished - Jan 2017

Publication series

NameRSC Metallobiology
Number9
Volume2017-January
ISSN (Print)2045547X

Fingerprint

Copper
Wolinella
Enzymes
Denitrification
Spectroscopic analysis
Nitrous Oxide
Sulfides
Sulfur
Gases
Metals
Electrons
Ligands
Atoms
Molecules
Water
nitrous oxide reductase
hydroxide ion

Keywords

  • copper
  • nitrous oxide
  • nitrous oxide reductase

Cite this

Pauleta, S. R., Carreira, C., & Moura, I. (2017). Insights into Nitrous Oxide Reductase. In Metalloenzymes in Denitrification: Applications and Environmental Impacts (Vol. 7, pp. 141-169). (RSC Metallobiology; Vol. 2017-January, No. 9). Royal Society of Chemistry. https://doi.org/10.1039/9781782623762-00141
Pauleta, Sofia R. ; Carreira, Cíntia ; Moura, Isabel. / Insights into Nitrous Oxide Reductase. Metalloenzymes in Denitrification: Applications and Environmental Impacts. Vol. 7 Royal Society of Chemistry, 2017. pp. 141-169 (RSC Metallobiology; 9).
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Pauleta, SR, Carreira, C & Moura, I 2017, Insights into Nitrous Oxide Reductase. in Metalloenzymes in Denitrification: Applications and Environmental Impacts. vol. 7, RSC Metallobiology, no. 9, vol. 2017-January, Royal Society of Chemistry, pp. 141-169. https://doi.org/10.1039/9781782623762-00141

Insights into Nitrous Oxide Reductase. / Pauleta, Sofia R.; Carreira, Cíntia; Moura, Isabel.

Metalloenzymes in Denitrification: Applications and Environmental Impacts. Vol. 7 Royal Society of Chemistry, 2017. p. 141-169 (RSC Metallobiology; Vol. 2017-January, No. 9).

Research output: Chapter in Book/Report/Conference proceedingChapter

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AB - 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.

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BT - Metalloenzymes in Denitrification

PB - Royal Society of Chemistry

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Pauleta SR, Carreira C, Moura I. Insights into Nitrous Oxide Reductase. In Metalloenzymes in Denitrification: Applications and Environmental Impacts. Vol. 7. Royal Society of Chemistry. 2017. p. 141-169. (RSC Metallobiology; 9). https://doi.org/10.1039/9781782623762-00141