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Manuela M. Pereira

Researcher at Universidade Nova de Lisboa

Publications -  96
Citations -  3555

Manuela M. Pereira is an academic researcher from Universidade Nova de Lisboa. The author has contributed to research in topics: Respiratory chain & Oxidoreductase. The author has an hindex of 31, co-authored 90 publications receiving 3258 citations. Previous affiliations of Manuela M. Pereira include University of Helsinki & University of Lisbon.

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The role of proton and sodium ions in energy transduction by respiratory complex I.

TL;DR: A hypothesis is put forward to explain some apparently contradictory data on the nature of the coupling ion, and the role of H+ and Na+ cycles in the overall bioenergetics of the cell is revisited.
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The key role of glutamate 172 in the mechanism of type II NADH:quinone oxidoreductase of Staphylococcus aureus.

TL;DR: The hypothesis for E172 being of central importance in the catalytic mechanism of NDH-2, which may be extended to other members of the two-Dinucleotide Binding Domains Flavoprotein superfamily, is supported.
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Electron transfer dynamics of Rhodothermus marinus caa3 cytochrome c domains on biomimetic films

TL;DR: The results indicate that the transient interaction between Cyt-D and HiPIP relies upon a delicate balance of hydrophobic and polar contacts for establishing an optimized electron transfer pathway that involves the exposed edge of the heme group and guaranties efficient inter-protein electron transfer on the nanosecond time scale.
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A nhaD Na+/H+ antiporter and a pcd homologues are among the Rhodothermus marinus complex I genes.

TL;DR: The open-reading-frames of the putative NhaD and PCD were shown to be co-transcribed with the other complex I genes encoded by nqoB, indicating the possible role of these two genes in R. marinus complex I.
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Ligand Binding and the Catalytic Reaction of Cytochrome caa3 from the Thermophilic Bacterium Rhodothermus marinus

TL;DR: The ligand-binding dynamics and the reaction with O(2) of the fully (five-electron) reduced cytochrome caa(3) from the thermohalophilic bacterium Rhodothermus (R.) marinus were investigated, finding the slower transition times as compared to those observed with the bovine enzyme most likely reflect the replacement of Glu(I-286) with a tyrosine in the R. marinus enzyme.