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Polar marine biology science in Portugal and Spain: Recent advances and future ...
Xavier, José C.; Barbosa, Andrés; Agustí, Susana; Alonso-Sáez, Laura; Alvito, Pedro; Ameneiro, Julia; Ávila, Conxita; Baeta, Alexandra; Canário, JoãoPolar marine ecosystems have global ecological and economic importance because of their unique biodiversity and their major role in climate processes and commercial fisheries, among others. Portugal and Spain have been highly active in a wide range of disciplines in marine biology of the Antarctic and the Arctic. The main aim of this paper is to provide a synopsis of some of the results and initiatives undertak...
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...
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...
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...
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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