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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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Observation of ligand-based redox chemistry at the active site of a molybdenum enzyme
TL;DR: In this article, the authors present an extended X-ray absorption fine structure (EXAFS) spectroscopic study of the molybdenum site of Desulfovibrio desulfuricans ATCC 27774 formate dehydrogenase (FDH) and show that under reducing conditions the selenosulfide group can be reduced.
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Effects of Molybdate and Tungstate on Expression Levels and Biochemical Characteristics of Formate Dehydrogenases Produced by Desulfovibrio alaskensis NCIMB 13491
Cristiano Mota,Odile Valette,Pablo J. González,Carlos D. Brondino,José J. G. Moura,Isabel Moura,Alain Dolla,Maria G. Rivas +7 more
TL;DR: The genes encoding the Mo/W-FDH are strongly downregulated by W and slightly upregulated by Mo, and the expression levels of the genes encoding proteins involved in molybdate and tungstate transport are downregulated under the experimental conditions evaluated in this work.
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Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase
Katja Conrath,Alice S. Pereira,Carlos E. Martins,Cristina G. Timóteo,Pedro Tavares,Silvia Spinelli,J. Kinne,Christophe Flaudrops,Christian Cambillau,Serge Muyldermans,Isabel Moura,José J. G. Moura,Mariella Tegoni,Aline Desmyter +13 more
TL;DR: The results indicate that VHHs are able to recognize with high affinity distinct epitopes on this class of proteins, and can be used as versatile and valuable tool for purification, functional study and crystallization of integral membrane proteins.
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The first crystal structure of class III superoxide reductase from Treponema pallidum
Teresa Santos-Silva,José Trincão,Ana Luísa Carvalho,Cecília Bonifácio,Françoise Auchère,Patrícia Raleiras,Isabel Moura,José J. G. Moura,Maria João Romão +8 more
TL;DR: Details in the TpSOR structure suggest that Lys49 might be involved in attraction of superoxide to the active site, and the overall architecture is very similar to that of other known SORs but Tp SOR contains an N-terminal domain in which the desulforedoxin-type Fe centre is absent.
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Low-spin sulfite reductases: A new homologous group of non-heme iron-siroheme proteins in anaerobic bacteria
TL;DR: The results suggest that the low molecular weight, low-spin non-heme iron siroheme proteins represent a new homologous class of sulfite reductases common to anaerobic microorganisms.