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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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Molybdenum and tungsten enzymes: the xanthine oxidase family.

TL;DR: Spectroscopic studies have provided an important amount of information on the characteristics of the active site and the electron transfer pathways of mononuclear Mo-containing enzymes.
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Cytochrome c Nitrite Reductase from Desulfovibrio desulfuricans ATCC 27774: THE RELEVANCE OF THE TWO CALCIUM SITES IN THE STRUCTURE OF THE CATALYTIC SUBUNIT (NrfA) *

TL;DR: The gene encoding cytochrome cnitrite reductase (NrfA) from Desulfovibrio desulfuricansATCC 27774 was sequenced and the crystal structure of the enzyme was determined, suggesting that the calcium ion at the distal side of the active site in the NrfA enzymes may have a similar physiological role to that reported for the peroxidases.
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Reduction of Carbon Dioxide by a Molybdenum-Containing Formate Dehydrogenase: A Kinetic and Mechanistic Study.

TL;DR: The ability of Desulfovibrio desulfuricans formate dehydrogenase (DdFDH) to reduce carbon dioxide was kinetically and mechanistically characterized and a kinetic model of a hysteretic enzyme is proposed to interpret and predict the progress curves of the Dd FDH-catalyzed reactions.
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Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus.

TL;DR: Ni and Se x-ray absorption spectroscopic studies of the [NiFeSe]hydrogenases from Desulfovibrio baculatus are described and the possible role of the Ni-Se site in the catalytic activation of H2 is discussed.
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Molybdenum and tungsten-dependent formate dehydrogenases

TL;DR: This review will highlight the present knowledge about the diverse physiological roles of FDH in prokaryotes, their modular structural organisation and active site structures and the mechanistic strategies followed to accomplish the formate oxidation.