@article {2355,
	title = {Molybdenum and tungsten enzymes: the xanthine oxidase family},
	journal = {Curr Opin Chem Biol},
	volume = {10},
	number = {2},
	year = {2006},
	note = {<p>1367-5931 (Print)1367-5931 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}tReview</p>
},
	month = {Apr},
	pages = {109-14},
	abstract = {<p>Mononuclear molybdenum and tungsten are found in the active site of a diverse group of enzymes that, in general, catalyze oxygen atom transfer reactions. Enzymes of the xanthine oxidase family are the best-characterized mononuclear Mo-containing enzymes. Several 3D structures of diverse members of this family are known. Recently, the structures of substrate-bound and arsenite-inhibited forms of two members of this family have also been reported. In addition, spectroscopic studies have been utilized to elucidate fine details that complement the structural information. Altogether, these studies have provided an important amount of information on the characteristics of the active site and the electron transfer pathways.</p>
},
	keywords = {Binding Sites, Electron Transport, Models, Molecular, Molybdenum/*metabolism, Protein Conformation, Tungsten/*metabolism, Xanthine Oxidase/antagonists \& inhibitors/chemistry/*metabolism},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=16480912 },
	author = {Brondino, C. D. and Romao, M. J. and Moura, I. and Moura, J. J.}
}
