@article {5326,
	title = {A novel type of catalytic copper cluster in nitrous oxide reductase},
	journal = {Nature Structural Biology},
	volume = {{7}},
	number = {{3}},
	year = {2000},
	note = {n/a},
	month = {Apr},
	pages = {{191-195}},
	publisher = {NATURE PUBLISHING GROUP},
	address = {75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA},
	abstract = {<p>Nitrous oxide (N(2)O) is a greenhouse gas, the third most significant contributor to global warming. As a key process for N(2)O elimination from the biosphere, N(2)O reductases catalyze the two-electron reduction of N(2)O to N(2). These 2 x 65 kDa copper enzymes are thought to contain a CuA electron entry site, similar to that of cytochrome c oxidase, and a CuZ catalytic center. The copper anomalous signal was used to solve the crystal structure of N(2)O reductase from Pseudomonas nautica by multiwavelength anomalous dispersion, to a resolution of 2.4 Angstrom. The structure reveals that the CuZ center belongs to a new type of metal cluster, in which four copper ions are liganded by seven histidine residues. N(2)O binds to this center via a single copper ion. The remaining copper ions might act as an electron reservoir, assuring a fast electron transfer and avoiding the formation of dead-end products.</p>
},
	author = {Brown, K. and Tegoni, M. and Prudencio, M. and Pereira, A. S. and Besson, S. and Moura, J. J. and Moura, I. and Cambillau, C.}
}
