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The mechanism of formate oxidation by metal-dependent formate dehydrogenases
Mota, Cristiano S.; Rivas, Maria G.; Brondino, Carlos D.; Moura, Isabel; Moura, José J. G.; González, Pablo J.; Cerqueira, Nuno M. F. S. A.J Biol Inorg Chem (2011) 16:1255–1268 DOI 10.1007/s00775-011-0813-8 ; 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 substr...
Effects of molybdate and tungstate on expression levels and biochemical charact...
Mota, Cristiano S.; Valette, Odile; J. González, Pablo; Brondino, Carlos D.; Moura, José J. G.; Moura, Isabel; Dolla, Alain; Rivas, Maria G.Journal of Bacteriology. 2011 Jun; Vol. 193 issue 12 pages 2917-2923 ; Formate dehydrogenases (FDHs) are enzymes that catalyze the formate oxidation to carbon dioxide and that contain either Mo or W in a mononuclear form in the active site. In the present work, the influence of Mo and W salts on the production of FDH by Desulfovibrio alaskensis NCIMB 13491 was studied. Two different FDHs, one containing W (W...
Molybdenum Induces the expression of a protein containing a new heterometallic ...
Rivas, Maria G.; Carepo, Marta S. P.; Mota, Cristiano S.; Moura, José J. G.; Moura, Isabel; Korbas, Malgorzata; Lopes, Ana T.; Brondino, Carlos D.Biochemistry. 2009 Feb 10;48(5):873-82. doi: 10.1021/bi801773t. ; The characterization of a novel Mo-Fe protein (MorP) associated with a system that responds to Mo in Desulfovibrio alaskensis is reported. Biochemical characterization shows that MorP is a periplasmic homomultimer of high molecular weight (260 +/- 13 kDa) consisting of 16-18 monomers of 15321.1 +/- 0.5 Da. The UV/visible absorption spectrum of t...
Structural and electron paramagnetic resonance (EPR) studies of mononuclear mol...
Brondino, Carlos D.; Rivas, Maria G.; Romão, Maria J.; Moura, José J. G.; Moura, IsabelAcc. Chem. Res., 2006, 39 (10), pp 788–796 DOI: 10.1021/ar050104k ; 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, aspa...
EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio de...
González, Pablo J.; Rivas, Maria G.; Brondino, Carlos D.; Bursakov, Sergey A.; Moura, Isabel; Moura, José J. G.J Biol Inorg Chem (2006) 11: 609–616 DOI 10.1007/s00775-006-0110-0 ; Nitrate reductases are enzymes that catalyze the conversion of nitrate to nitrite. We report here electron paramagnetic resonance (EPR) studies in the periplasmic nitrate reductase isolated from the sulfate-reducing bacteria Desulfovibrio desulfuricans ATCC 27774. This protein, belonging to the dimethyl sulfoxide reductase family of mononucle...
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