@article {2408,
	title = {Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas},
	journal = {Structure},
	volume = {10},
	number = {9},
	year = {2002},
	note = {<p>0969-2126 (Print)0969-2126 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Sep},
	pages = {1261-72},
	abstract = {<p>Desulfovibrio gigas formate dehydrogenase is the first representative of a tungsten-containing enzyme from a mesophile that has been structurally characterized. It is a heterodimer of 110 and 24 kDa subunits. The large subunit, homologous to E. coli FDH-H and to D. desulfuricans nitrate reductase, harbors the W site and one [4Fe-4S] center. No small subunit ortholog containing three [4Fe-4S] clusters has been reported. The structural homology with E. coli FDH-H shows that the essential residues (SeCys158, His159, and Arg407) at the active site are conserved. The active site is accessible via a positively charged tunnel, while product release may be facilitated, for H(+) by buried waters and protonable amino acids and for CO(2) through a hydrophobic channel.</p>
},
	keywords = {Amino Acid Sequence, Binding Sites, Carbon Dioxide/metabolism, Crystallography, X-Ray, Desulfovibrio/*enzymology/genetics, Electrons, Formate Dehydrogenases/*chemistry/genetics/*metabolism, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Subunits/chemistry/metabolism, Protons, Sequence Homology, Amino Acid, Static Electricity, Structure-Activity Relationship, Tungsten/*metabolism},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=12220497 },
	author = {Raaijmakers, H. and Macieira, S. and Dias, J. M. and Teixeira, S. and Bursakov, S. and Huber, R. and Moura, J. J. and Moura, I. and Romao, M. J.}
}
