@article {2425,
	title = {Structural aspects of denitrifying enzymes},
	journal = {Curr Opin Chem Biol},
	volume = {5},
	number = {2},
	year = {2001},
	note = {<p>1367-5931 (Print)1367-5931 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}tReview</p>
},
	month = {Apr},
	pages = {168-75},
	abstract = {<p>The reduction of nitrate to nitrogen gas via nitrite, nitric oxide and nitrous oxide is the metabolic pathway usually known as denitrification, a key step in the nitrogen cycle. As observed for other elemental cycles, a battery of enzymes are utilized, namely the reductases for nitrate, nitrite, nitric oxide and nitrous oxide, as well as multiple electron donors that interact with these enzymes, in order to carry out the stepwise reactions that involve key intermediates. Because of the importance of this pathway (of parallel importance to the nitrogen-fixation pathway), efforts are underway to understand the structures of the participating enzymes and to uncover mechanistic aspects. Three-dimensional structures have been solved for the majority of these enzymes in the past few years, revealing the architecture of the active metal sites as well as global structural aspects, and possible mechanistic aspects. In addition, the recognition of specific electron-transfer partners raises important questions regarding specific electron-transfer pathways, partner recognition and control of metabolism.</p>
},
	keywords = {Electron Transport, Enzymes/*chemistry/metabolism, Metalloproteins/chemistry, Models, Molecular, Nitrate Reductases/*chemistry/metabolism, Nitric Oxide/metabolism, Nitrite Reductases/*chemistry/metabolism, Nitrous Oxide/metabolism, Oxidoreductases/*chemistry/metabolism, Protein Structure, Tertiary},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=11282344 },
	author = {Moura, I. and Moura, J. J.}
}
