@article {2265,
	title = {The mechanism of formate oxidation by metal-dependent formate dehydrogenases},
	journal = {J Biol Inorg Chem},
	volume = {16},
	number = {8},
	year = {2011},
	note = {<p>1432-1327 (Electronic)0949-8257 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Dec},
	pages = {1255-68},
	abstract = {<p>Metal-dependent formate dehydrogenases (Fdh) from prokaryotic organisms are members of the dimethyl sulfoxide reductase family of mononuclear molybdenum-containing and tungsten-containing enzymes. Fdhs catalyze the oxidation of the formate anion to carbon dioxide in a redox reaction that involves the transfer of two electrons from the substrate to the active site. The active site in the oxidized state comprises a hexacoordinated molybdenum or tungsten ion in a distorted trigonal prismatic geometry. Using this structural model, we calculated the catalytic mechanism of Fdh through density functional theory tools. The simulated mechanism was correlated with the experimental kinetic properties of three different Fdhs isolated from three different Desulfovibrio species. Our studies indicate that the C-H bond break is an event involved in the rate-limiting step of the catalytic cycle. The role in catalysis of conserved amino acid residues involved in metal coordination and near the metal active site is discussed on the basis of experimental and theoretical results.</p>
},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=21773834 },
	author = {Mota, C. S. and Rivas, M. G. and Brondino, C. D. and Moura, I. and Moura, J. J. and Gonzalez, P. J. and Cerqueira, N. M.}
}
