<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>13</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Pauleta, S. R.</style></author><author><style face="normal" font="default" size="100%">Carreira, C.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author></authors><secondary-authors><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Garner, C. D.</style></author><author><style face="normal" font="default" size="100%">Pauleta, S. R.</style></author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">CHAPTER 7: Insights into Nitrous Oxide Reductase</style></title><secondary-title><style face="normal" font="default" size="100%">RSC Metallobiology</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.scopus.com/inward/record.uri?eid=2-s2.0-85006272405&amp;doi=10.1039%2f9781782623762-00141&amp;partnerID=40&amp;md5=4f11e02bd7a4da983b55330ab3e0e33c</style></url></web-urls></urls><publisher><style face="normal" font="default" size="100%">Royal Society of Chemistry</style></publisher><volume><style face="normal" font="default" size="100%">2017-January</style></volume><pages><style face="normal" font="default" size="100%">141-169</style></pages><isbn><style face="normal" font="default" size="100%">2045547X (ISSN)</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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 &quot;CuZ centre&quot;, located in different domains. The CuA centre is the electron transferring centre, while the catalytic centre is the &quot;CuZ centre&quot;, a unique metal centre in biology - a tetranuclear copper centre with a μ4-bridging sulphide. The enzyme has been isolated with the &quot;CuZ centre&quot; 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 &quot;CuZ centre&quot;, 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 &quot;atypical&quot;, with a single member of the last group having been isolated to date, from Wolinella succinogenes. Thus, here the structure of the &quot;typical&quot; nitrous oxide reductase with either CuZ(4Cu2S) or CuZ∗(4Cu1S), as well as its spectroscopic and catalytic properties, will be discussed. © The Royal Society of Chemistry 2017.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Book Chapter</style></work-type><notes><style face="normal" font="default" size="100%">&lt;p&gt;Export Date: 31 January 2017&lt;/p&gt;
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