P
Pedro Tavares
Researcher at Universidade Nova de Lisboa
Publications - 67
Citations - 1953
Pedro Tavares is an academic researcher from Universidade Nova de Lisboa. The author has contributed to research in topics: Rubredoxin & Desulfovibrio. The author has an hindex of 23, co-authored 62 publications receiving 1836 citations. Previous affiliations of Pedro Tavares include North Carolina State University & Massachusetts Institute of Technology.
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Journal ArticleDOI
Metalloenzymes of the denitrification pathway.
TL;DR: This manuscript presents a concise updated review of the bioinorganic aspects of denitrification, an anaerobic process used by some bacteria for energy generation and its environmental implications have been given particular relevance.
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Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization
Alice S. Pereira,William C. Small,Carsten Krebs,Pedro Tavares,Dale E. Edmondson,Elizabeth C. Theil,Boi Hanh Huynh +6 more
TL;DR: The proposal that a single protein site, with a structure homologous to the diiron centers in MMOH and R2, is involved in the ferritin ferroxidation step is confirmed by the observed kinetics, spectroscopic properties, and purity of the initial peroxodiferric species formed in the frog M ferritIn.
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Mössbauer characterization of the iron-sulfur clusters in Desulfovibrio vulgaris hydrogenase.
TL;DR: Variable-temperature and variable-field Mössbauer spectroscopy has been used to characterize the Fe-S clusters in D. vulgaris hydrogenase, revealing that binding of exogenous CO to the H cluster affects significantly the exchange coupling between the [4Fe-4S] and the [2Fe](H) subclusters.
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Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center.
TL;DR: Mössbauer data indicates the presence of two types of iron: an FeS4 site very similar to that found in desulforedoxin from Desulfovibrio gigas and an octahedral coordinated high-spin ferrous site most probably with nitrogen/oxygen-containing ligands.
Journal ArticleDOI
Purification, characterization, and preliminary crystallographic study of copper-containing nitrous oxide reductase from Pseudomonas nautica 617.
Miguel Prudêncio,Alice S. Pereira,Pedro Tavares,Stéphane Besson,Inês Cabrito,K. Brown,B Samyn,Bart Devreese,J. Van Beeumen,Frank Rusnak,G. Fauque,José J. G. Moura,M. Tegoni,C. Cambillau,Isabel Moura +14 more
TL;DR: The aerobic purification of Pseudomonas nautica 617 nitrous oxide reductase yielded two forms of the enzyme exhibiting different chromatographic behaviors, interpreted as a difference in the oxidation state of the Cu(A) center.