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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...
Crystallization and crystallographic analysis of the apo form of the orange pro...
Najmudin, Shabir; Bonifácio, Cecília; Duarte, Américo G.; Pualeta, Sofia R.; Moura, Isabel; Moura, José J. G.; Romão, Maria J.Acta Crystallographica Section F Structural Biology and Crystallization Communications Volume 65, Part 8 ; The orange-coloured protein (ORP) from Desulfovibrio gigas is a 12 kDa protein that contains a novel mixed-metal sulfide cluster of the type [S2MoS2-CuS2MoS2]. Diffracting crystals of the apo form of ORP have been obtained. Data have been collected for the apo form of ORP to 2.25 A ° resolution in-house a...
Purification, crystallization and preliminary X-ray diffraction analysis of ade...
Gavel, Olga Yu.; Kladova, Anna V.; Bursakov, Sergey A.; Dias, João M.; Texeira, Susana; Moura, José J. G.; Moura, Isabel; Romão, Maria J.; Trincão, JoséActa Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt 7):593-5 ; Native zinc/cobalt-containing ATP sulfurylase (ATPS; EC 2.7.7.4; MgATP: sulfate adenylyltransferase) from Desulfovibrio desulfuricans ATCC 27774 was purified to homogeneity and crystallized. The orthorhombic crystals diffracted to beyond 2.5 A ° resolution and the X-ray data collected should allow the determination of the structure o...
Heterodimeric nitrate reductase (NapAB) from Cupriavidus necator H16: purificat...
Coelho, Catarina; J. Gonzaléz, Pablo; Trincão, José; Carvalho, Ana L.; Najmudin, Shabir; Moura, José J. G.; Hettman, Thomas; Dieckman, StephanActa Cryst. (2007). F63, 516–519 ; The periplasmic nitrate reductase from Cupriavidus necator (also known as Ralstonia eutropha) is a heterodimer that is able to reduce nitrate to nitrite. It comprises a 91 kDa catalytic subunit (NapA) and a 17 kDa subunit (NapB) that is involved in electron transfer. The larger subunit contains a molybdenum active site with a bis-molybdopterin guanine dinucleotide cofactor as...
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...
The first crystal structure of class III superoxide reductase from Treponema pa...
Santos-Silva, Teresa; Trincão, José; Carvalho, Ana Luísa; Bonifácio, Cecília; Auchère, Françoise; Raleiras, Patrícia; Moura, Isabel; Moura, José J. G.J Biol Inorg Chem (2006) 11: 548–558 DOI 10.1007/s00775-006-0104-y ; Superoxide reductase (SOR) is a metalloprotein containing a non-heme iron centre, responsible for the scavenging of superoxide radicals in the cell. The crystal structure of Treponema pallidum (Tp) SOR was determined using soft X-rays and synchrotron radiation. Crystals of the oxidized form were obtained using poly(ethylene glycol) and MgCl2 ...
Superoxide reductase from the syphilis spirochete Treponema pallidum
Moura, Isabel; Santos-Silva, Teresa; Trincão, José; Carvalho, Ana L.; Auchère, Françoise; Moura, José J. G.; Romão, Maria J.Superoxide reductase is a 14 kDa metalloprotein containing a catalytic nonhaem iron centre [Fe(His)4Cys]. It is involved in defence mechanisms against oxygen toxicity, scavenging superoxide radicals from the cell. The oxidized form of Treponema pallidum superoxide reductase was crystallized in the presence of polyethylene glycol and magnesium chloride. Two crystal forms were obtained depending on the oxidizing ...
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...
X-ray crystal structure and EPR spectra of "arsenite-inhibited" Desulfovibriogi...
Boer, D. Roeland; Thapper, Anders; Brondino, Carlos D.; Romão, Maria J.; Moura, José J. G.J. Am. Chem. Soc., 2004, 126 (28), pp 8614–8615 DOI: 10.1021/ja0490222 ; X-ray crystallography has been used to determine the structure of arsenite-inhibited aldehyde dehydrogenase from Desulfovibrio gigas, a member of the xanthine oxidase family of mononuclear molybdenum enzymes. The structure shows an AsO3 moiety bound to the molybdenum atom of the active site through one of the oxygen atoms. A reduced sampl...
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