@article {10114,
	title = {Nitrous oxide reductase},
	journal = {Coordination Chemistry Reviews},
	volume = {257},
	number = {2},
	year = {2013},
	note = {<p>Times Cited: 0 Pauleta, Sofia R. Dell{\textquoteright}Acqua, Simone Moura, Isabel SI</p>
},
	month = {Jan},
	pages = {332-349},
	abstract = {<p>Nitrous oxide is a potent greenhouse gas, whose atmospheric concentration has been increasing since the introduction of the Haber Bosch process led to the widespread use of nitrogenous fertilizers. One of the pathways to its destruction is reduction to molecular nitrogen by the enzyme nitrous oxide reductase found in denitrifying bacteria. This enzyme catalyzes the last step of the denitrification pathway. It has two copper centers, a binuclear CuA center, similar to the one found in cytochrome c oxidase, and the CuZ center, a unique tetranuclear copper center now known to possess either one or two sulfide bridges. Nitrous oxide reductase has been isolated in different forms, depending on the oxidation state and molecular forms of its Cu centers. Recently, the structure of a purple form, which has both centers in the oxidized state, revealed that the CuZ center has the form [Cu4S2]. This review summarizes the biogenesis and regulation of nitrous oxide reductase, and the spectroscopic and kinetic properties of nitrous oxide reductase. The proposed activation and catalytic mechanism, as well as, electron transfer pathways are discussed in the light of the various structures of the CuZ center. (C) 2012 Published by Elsevier B.V.</p>
},
	isbn = {0010-8545},
	url = {<Go to ISI>://WOS:000312762200003},
	author = {Pauleta, S. R. and Dell{\textquoteright}acqua, S. and Moura, I}
}
