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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, José

Acta 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...

Data: 2008   |   Origem: Repositório Institucional da UNL

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...

Data: 2006   |   Origem: Repositório Institucional da UNL

Structural stability of adenylate kinase from the sulfate-reducing bacteria Des...

Moura, José J. G.; Moura, Isabel; Gavel, Olga Yu.; Bursakov, Sergey A.; Pina, David G.; Zhadan, Galina G.; Shnyrov, Valery L.

Biophysical Chemistry 110 (2004) 83–92 ; A novel adenylate kinase (AK) has recently been purified from Desulfovibrio gigas and characterized as a Co2+/Zn2+-containing enzyme: this is an unusual characteristic for AKs from Gram-negative bacteria, in which these enzymes are normally devoid of metals. Here, we studied the conformational stability of holo- and apo-AK as a function of temperature by differential sc...

Data: 2004   |   Origem: Repositório Institucional da UNL

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Fundação para a Ciência e a Tecnologia Universidade do Minho   Governo Português Ministério da Educação e Ciência Programa Operacional da Sociedade do Conhecimento União Europeia