@booklet {10130,
	title = {CHAPTER 7: Insights into Nitrous Oxide Reductase},
	journal = {RSC Metallobiology},
	volume = {2017-January},
	year = {2017},
	note = {<p>Export Date: 31 January 2017</p>
},
	pages = {141-169},
	publisher = {Royal Society of Chemistry},
	type = {Book Chapter},
	abstract = {<p>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. {\textcopyright} The Royal Society of Chemistry 2017.</p>
},
	isbn = {2045547X (ISSN)},
	url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85006272405\&doi=10.1039\%2f9781782623762-00141\&partnerID=40\&md5=4f11e02bd7a4da983b55330ab3e0e33c},
	author = {Pauleta, S. R. and Carreira, C. and Moura, I},
	editor = {Moura, I and Moura, JJG and Maia, L. B. and Garner, C. D. and Pauleta, S. R.}
}
