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Isabel Moura
Researcher at Universidade Nova de Lisboa
Publications - 421
Citations - 14404
Isabel Moura is an academic researcher from Universidade Nova de Lisboa. The author has contributed to research in topics: Desulfovibrio gigas & Rubredoxin. The author has an hindex of 61, co-authored 420 publications receiving 13481 citations. Previous affiliations of Isabel Moura include University of Vigo & University of New Mexico.
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Purification and characterization of a tungsten-containing formate dehydrogenase from Desulfovibrio gigas.
M. J. Almendra,Carlos D. Brondino,Olga Yu. Gavel,Alice S. Pereira,Pedro Tavares,Sergey A. Bursakov,Rui O. Duarte,Jorge Caldeira,José J. G. Moura,Isabel Moura +9 more
TL;DR: Variable-temperature EPR studies showed the presence of two signals compatible with an atom in a d(1) configuration albeit with an unusual relaxation behavior as compared to the one generally observed for W(V) ions.
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Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774.
Jorge Rebelo,Sofia Macieira,Sofia Macieira,João M. Dias,Robert Huber,Carla Ascenso,Carla Ascenso,Frank Rusnak,José J. G. Moura,Isabel Moura,Maria João Romão +10 more
TL;DR: In this paper, aldehyde oxidoreductase (MOD) isolated from the sulfate reducer Desulfovibrio desulfuricans (ATCC 27774) is a member of the xanthine oxidase family of molybdenum-containing enzymes.
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The isolation and characterization of cytochrome c nitrite reductase subunits (NrfA and NrfH) from Desulfovibrio desulfuricans ATCC 27774. Re-evaluation of the spectroscopic data and redox properties.
Maria Gabriela Almeida,Sofia Macieira,Luísa L. Gonçalves,Robert Huber,Carlos A. Cunha,Maria João Romão,Cristina Costa,Jorge Lampreia,José J. G. Moura,Isabel Moura +9 more
TL;DR: The cytochrome c nitrite reductase is isolated from the membranes of the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 as a heterooligomeric complex composed by two subunits containing c-type hemes, encoded by the genes nrfA and nrfH.
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Mammalian ferrochelatase, a new addition to the metalloenzyme family.
Gloria C. Ferreira,Ricardo Franco,Steven G. Lloyd,Alice S. Pereira,Isabel Moura,José J. G. Moura,Boi Hanh Huynh +6 more
TL;DR: The putative protein binding site for the Fe-S cluster in mammalian ferrochelatases is absent from the sequences of the bacterial and yeast enzymes, suggesting a possible role of the [2Fe-2S] center in regulation of mammalian ferrifying enzymes.
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Characterization of two dissimilatory sulfite reductases (desulforubidin and desulfoviridin) from the sulfate-reducing bacteria. Moessbauer and EPR studies
Isabel Moura,Jean LeGall,A. R. Lino,Harry D. Peck,G. Fauque,António V. Xavier,Daniel V. DerVartanian,José J. G. Moura,B.H. Huynh +8 more
TL;DR: In this paper, a detailed Moessbauer investigation of two different sulfite reductases, namely, desulforubidin from D. baculatus and desulfoviridin, was performed.