@article {2356,
	title = {Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria},
	journal = {Acc Chem Res},
	volume = {39},
	number = {10},
	year = {2006},
	note = {<p>0001-4842 (Print)0001-4842 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}tReview</p>
},
	month = {Oct},
	pages = {788-96},
	abstract = {<p>Molybdenum and tungsten are found in biological systems in a mononuclear form in the active site of a diverse group of enzymes that generally catalyze oxygen-atom-transfer reactions. The metal atom (Mo or W) is coordinated to one or two pyranopterin molecules and to a variable number of ligands such as oxygen (oxo, hydroxo, water, serine, aspartic acid), sulfur (cysteines), and selenium (selenocysteines) atoms. In addition, these proteins contain redox cofactors such as iron-sulfur clusters and heme groups. All of these metal cofactors are along an electron-transfer pathway that mediates the electron exchange between substrate and an external electron acceptor (for oxidative reactions) or donor (for reductive reactions). We describe in this Account a combination of structural and electronic paramagnetic resonance studies that were used to reveal distinct aspects of these enzymes.</p>
},
	keywords = {Aldehyde Oxidoreductases/genetics/metabolism, Bacteria/*enzymology, Binding Sites, Electron Spin Resonance Spectroscopy, Enzyme Inhibitors/chemistry/pharmacology, Enzymes/*chemistry/genetics, Formate Dehydrogenases/genetics/metabolism, Models, Molecular, Molybdenum/*chemistry, Stereoisomerism, Sulfates/*metabolism},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=17042479 },
	author = {Brondino, C. D. and Rivas, M. G. and Romao, M. J. and Moura, J. J. and Moura, I.}
}
