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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...
Kinetic, Structural, and EPR Studies Reveal That Aldehyde Oxidoreductase from D...
Silva, Teresa Santos; Ferroni, Felix; Thapper, Anders; Marangon, Jacopo; Moura, Isabel; Moura, José J. G.; Rizzi, Alberto C.; González, Pablo J.J. Am. Chem. Soc., 2009, 131 (23), pp 7990–7998 DOI: 10.1021/ja809448r ; Aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is a member of the xanthine oxidase(XO) family of mononuclear Mo-enzymes that catalyzes the oxidation of aldehydes to carboxylic acids. The molybdenum site in the enzymes of the XO family shows a distorted square pyramidal geometry in which two ligands, a hydroxyl/water molecule (th...
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...
Biochemical and spectroscopic characterization of the membrane-bound nitrate re...
Correia, Cristina; Besson, Stéphane; Brondino, Carlos D.; González, Pablo J.; Lampreia, Jorge; Moura, Isabel; Moura, José J. G.J Biol Inorg Chem (2008) 13:1321–1333 DOI 10.1007/s00775-008-0416-1 ; Membrane-bound nitrate reductase from Marinobacter hydrocarbonoclasticus 617 can be solubilized in either of two ways that will ultimately determine the presence or absence of the small (Iota) subunit. The enzyme complex (NarGHI) is composed of three subunits with molecular masses of 130, 65, and 20 kDa. This enzyme contains approximately 14...
Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of al...
Thapper, Anders; Boer, D. R.; Brondino, Carlos D.; Moura, José J. G.; Romão, Maria J.J Biol Inorg Chem (2007) 12:353–366 DOI 10.1007/s00775-006-0191-9 ; Two arsenite-inhibited forms of each of the aldehyde oxidoreductases from Desulfovibrio gigas and Desulfovibrio desulfuricans have been studied by X-ray crystallography and electron paramagnetic resonance (EPR) spectroscopy. The molybdenum site of these enzymes shows a distorted square-pyramidal geometry in which two ligands, a hydroxyl/water ...
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...
Copper complexes with new oxaaza-pendant-armed macrocyclic ligands: X-ray cryst...
Vicente, Manuel; Bastida, Rufina; Macías, Alejandro; Valencia, Laura; Geraldes, Carlos F. G. C.; Brondino, Carlos D.The synthesis of new oxaaza macrocyclic ligands (2-4) derived from O1,O7-bis(2-formylphenyl)-1,4,7-trioxaheptane and functionalized tris(2-aminoethyl)amine are described. Mononuclear copper(II) complexes were isolated in the reaction of the corresponding macrocyclic ligand and copper(II) perchlorate. The structure of the [Cu(2)](ClO4)2 complex was determined by X-ray diffraction analysis. The copper(II) ion is ...
Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases
Moura, José J. G.; Brondino, Carlos D.; Trincão, José; Romão, Maria J.J Biol Inorg Chem (2004) 9: 791–799 DOI 10.1007/s00775-004-0573-9 ; Molybdenum and tungsten are second- and third-row transition elements, respectively, which are found in a mononuclear form in the active site of a diverse group of enzymes that generally catalyze oxygen atom transfer reactions. Mononuclear Mo-containing enzymes have been classified into three families: xanthine oxidase, DMSO reductase, and sul...
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