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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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Identification of three classes of hydrogenase in the genus, Desulfovibrio.
Benet C. Prickril,Shao-Hua He,Ching Li,Nanda K. Menon,Eui-Sung Choi,Alan Przybyla,Daniel V. DerVartanian,Harry D. Peck,Guy Fauque,Jean LeGall,Miguel Teixeira,Isabel Moura,José J. G. Moura,D.S. Patil,Boi H. Huynh +14 more
TL;DR: A comparison of amino-terminal amino acid sequences from the large and small subunits of hydrogenases from Desulfovibrio reveals significant differences in amino acid sequence as mentioned in this paper.
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1H NMR spectra of rubredoxins: new resonances assignable to α-CH and β-CH2 hydrogens of cysteinate ligands to iron(II)
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NMR and electron-paramagnetic-resonance studies of a dihaem cytochrome from Pseudomonas stutzeri (ATCC 11607) (cytochrome c peroxidase)
Jose Villalaín,Isabel Moura,Ming-Cheh Liu,William J. Payne,Jean LeGall,António V. Xavier,José J. G. Moura +6 more
TL;DR: The NMR data fully support the haem-haem interaction probed by EPR, and indicates that for one of the haems a high-spin to low-spin transition is observed when temperature is decreased.
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Source and reduction of nitrous oxide
TL;DR: In this paper, a structural and functional model of the N2OR active site has been presented, where the reduction of nitrous oxide occurs in a unique catalytic tetranuclear sulfide center, named CuZ center, a complex center required to overcome the high activation barrier of this reaction.
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Electron transport in sulfate-reducing bacteria. Molecular modeling and NMR studies of the rubredoxin--tetraheme-cytochrome-c3 complex.
David E. Stewart,Jean LeGall,Isabel Moura,Isabel Moura,José J. G. Moura,José J. G. Moura,Harry D. Peck,António V. Xavier,Paul K. Weiner,John E. Wampler +9 more
TL;DR: A hypothetical model of the complex formed between the iron-sulfur protein rubredoxin and the tetraheme cy tochrome c3 from the sulfate-reducing bacteria Desulfovibrio vulgaris (Hildenborough) has been proposed utilizing computer graphic modeling, computational methods and NMR spectroscopy and new NMR data shows that both proteins interact with the same heme group of the cytochrome as postulated.