M
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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Journal ArticleDOI
A ba3 oxygen reductase from the thermohalophilic bacterium Rhodothermus marinus
Andreia F. Verissimo,Manuela M. Pereira,Ana M.P. Melo,Ana M.P. Melo,Gudmundur O. Hreggvidsson,Jakob K. Kristjansson,Miguel Teixeira +6 more
TL;DR: The isolation and characterization of a third oxygen reductase expressed in the thermohalophilic bacterium Rhodothermus marinus is described, showing 43% amino acid sequence identity and 63% similarity with the ba3 oxygen reduCTase from Thermus thermophilus.
Journal ArticleDOI
Active site structure of the aa3 quinol oxidase of Acidianus ambivalens.
Tapan K. Das,Cláudio M. Gomes,Tiago M. Bandeiras,Manuela M. Pereira,Miguel Teixeira,Denis L. Rousseau +5 more
TL;DR: A resonance Raman spectroscopic study of the aa(3)-type quinol:oxygen oxidoreductase from the hyperthermophilic archaeon, Acidianus ambivalens, showed that the pH dependence and H/D exchange demonstrate that the conformational transition is associated with proton movements involving a group or groups with a pK(a) of approximately 3.8.
Journal ArticleDOI
A ferredoxin from the thermohalophilic bacterium Rhodothermus marinus.
Manuela M. Pereira,Kathryn Jones,Marta Campos,Ana M.P. Melo,Ana M.P. Melo,Lígia M. Saraiva,Ricardo O. Louro,Pernilla Wittung-Stafshede,Miguel Teixeira +8 more
TL;DR: A small protein isolated from the thermohalophilic and strict aerobic bacterium Rhodothermus marinus, which contains a single, homogeneous, trinuclear centre, is investigated and is very sensitive to oxygen, an unexpected characteristic for a protein from an aerobic organism.
Journal ArticleDOI
The removal of a disulfide bridge in CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability
André T. Fernandes,Manuela M. Pereira,Catarina Silva,Peter F. Lindley,Peter F. Lindley,Isabel Bento,Eduardo P. Melo,Lígia O. Martins +7 more
TL;DR: Overall the structural and kinetic data presented here suggest that the disulfide bridge in CotA-laccase contributes to the conformational dynamics of the protein on the microsecond to millisecond timescale, with implications for the rates of copper incorporation into and release from the catalytic centres.
Journal ArticleDOI
A synthesis of the amaryllidaceae alkaloid pratosine
TL;DR: A synthesis of pratosine by thermolysis of the Michael adduct obtained from 5-hydroxy-8,9-dimethoxy-6(5H)-phenanthridone and methyl propiolate is described.