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.
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