@article {2444,
	title = {A novel type of catalytic copper cluster in nitrous oxide reductase},
	journal = {Nat Struct Biol},
	volume = {7},
	number = {3},
	year = {2000},
	note = {<p>1072-8368 (Print)1072-8368 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Mar},
	pages = {191-5},
	abstract = {<p>Nitrous oxide (N20) is a greenhouse gas, the third most significant contributor to global warming. As a key process for N20 elimination from the biosphere, N20 reductases catalyze the two-electron reduction of N20 to N2. 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 N20 reductase from Pseudomonas nautica by multiwavelength anomalous dispersion, to a resolution of 2.4 A. 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. N20 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>
},
	keywords = {Amino Acid Sequence, Azurin/analogs \& derivatives/metabolism, Binding Sites, Catalytic Domain, Copper/*chemistry/*metabolism, Crystallography, X-Ray, Dimerization, Histidine/metabolism, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Nitrous Oxide/metabolism, Oxidation-Reduction, Oxidoreductases/*chemistry/*metabolism, Protein Conformation, Protein Folding, Pseudomonas/*enzymology, Structure-Activity Relationship},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=10700275 },
	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.}
}
