M M Pereira

Summary

Affiliation: Universidade Nova de Lisboa
Country: Portugal

Publications

  1. pmc Thermodynamic redox behavior of the heme centers in A-type heme-copper oxygen reductases: comparison between the two subfamilies
    Andreia F Veríssimo
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Oeiras, Portugal
    Biophys J 95:4448-55. 2008
  2. pmc A bioinformatics classifier and database for heme-copper oxygen reductases
    Filipa L Sousa
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Oeiras, Portugal
    PLoS ONE 6:e19117. 2011
  3. ncbi request reprint A novel scenario for the evolution of haem-copper oxygen reductases
    M M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780 156, Oeiras, Portugal
    Biochim Biophys Acta 1505:185-208. 2001
  4. ncbi request reprint Looking for the minimum common denominator in haem-copper oxygen reductases: towards a unified catalytic mechanism
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica EAN, 2780 157 Oeiras, Portugal
    Biochim Biophys Acta 1777:929-34. 2008
  5. ncbi request reprint The alternative complex III from Rhodothermus marinus - a prototype of a new family of quinol:electron acceptor oxidoreductases
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica EAN, Apt 127, 2780 901 Oeiras, Portugal
    FEBS Lett 581:4831-5. 2007
  6. ncbi request reprint Is a Q-cycle-like mechanism operative in dihaemic succinate:quinone and quinol:fumarate oxidoreductases?
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780 156, Oeiras, Portugal
    FEBS Lett 543:1-4. 2003
  7. pmc Gene cluster of Rhodothermus marinus high-potential iron-sulfur Protein: oxygen oxidoreductase, a caa(3)-type oxidase belonging to the superfamily of heme-copper oxidases
    M Santana
    , Universidade Nova de Lisboa, 2780-156 Oeiras, Portugal
    J Bacteriol 183:687-99. 2001
  8. ncbi request reprint A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa Av da República, Apartado 127, 2781 901 Oeiras, Portugal
    FEBS Lett 580:1350-4. 2006
  9. doi request reprint The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
    Zhenjia Chen
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica, 2781 901, Oeiras, Portugal
    Dalton Trans 39:2875-82. 2010
  10. ncbi request reprint The succinate dehydrogenase from the thermohalophilic bacterium Rhodothermus marinus: redox-Bohr effect on heme bL
    A S Fernandes
    , Universidade Nova de Lisboa, Oeiras, Portugal
    J Bioenerg Biomembr 33:343-52. 2001

Collaborators

Detail Information

Publications37

  1. pmc Thermodynamic redox behavior of the heme centers in A-type heme-copper oxygen reductases: comparison between the two subfamilies
    Andreia F Veríssimo
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Oeiras, Portugal
    Biophys J 95:4448-55. 2008
    ..The results presented here for these A-type enzymes are compared with those previously obtained for representative members of the B and C families...
  2. pmc A bioinformatics classifier and database for heme-copper oxygen reductases
    Filipa L Sousa
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Oeiras, Portugal
    PLoS ONE 6:e19117. 2011
    ..These enzymes were initially classified into three different types being this classification recently challenged...
  3. ncbi request reprint A novel scenario for the evolution of haem-copper oxygen reductases
    M M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780 156, Oeiras, Portugal
    Biochim Biophys Acta 1505:185-208. 2001
    ..As the families of haem-copper oxidases can also be identified by their subunit II, a parallel evolution of subunits I and II is suggested...
  4. ncbi request reprint Looking for the minimum common denominator in haem-copper oxygen reductases: towards a unified catalytic mechanism
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica EAN, 2780 157 Oeiras, Portugal
    Biochim Biophys Acta 1777:929-34. 2008
    ....
  5. ncbi request reprint The alternative complex III from Rhodothermus marinus - a prototype of a new family of quinol:electron acceptor oxidoreductases
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica EAN, Apt 127, 2780 901 Oeiras, Portugal
    FEBS Lett 581:4831-5. 2007
    ..In this report, we establish undoubtedly the existence of an alternative complex III, a functional substitute of the bc(1) complex, by its identification at both the biochemical and genomic level...
  6. ncbi request reprint Is a Q-cycle-like mechanism operative in dihaemic succinate:quinone and quinol:fumarate oxidoreductases?
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780 156, Oeiras, Portugal
    FEBS Lett 543:1-4. 2003
    ..With this testable hypothesis we intend to challenge the discussion and drive further experimentation to unravel the functional mechanism of SQRs and QFRs...
  7. pmc Gene cluster of Rhodothermus marinus high-potential iron-sulfur Protein: oxygen oxidoreductase, a caa(3)-type oxidase belonging to the superfamily of heme-copper oxidases
    M Santana
    , Universidade Nova de Lisboa, 2780-156 Oeiras, Portugal
    J Bacteriol 183:687-99. 2001
    ..The data are discussed in the framework of the evolution of oxidases within the superfamily of heme-copper oxidases...
  8. ncbi request reprint A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa Av da República, Apartado 127, 2781 901 Oeiras, Portugal
    FEBS Lett 580:1350-4. 2006
    ..Comparison with the mitochondrial like oxygen reductase from Rhodobacter sphaeroides suggests that proton transfer from a strategically situated donor to the active site is a crucial step in the reaction mechanism of oxygen reductases...
  9. doi request reprint The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
    Zhenjia Chen
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica, 2781 901, Oeiras, Portugal
    Dalton Trans 39:2875-82. 2010
    ..Overall, the results strongly suggest that Glu(498) plays a key role in the protonation events that occur at the trinuclear centre and in its stabilization, controlling therefore the binding of dioxygen and its further reduction...
  10. ncbi request reprint The succinate dehydrogenase from the thermohalophilic bacterium Rhodothermus marinus: redox-Bohr effect on heme bL
    A S Fernandes
    , Universidade Nova de Lisboa, Oeiras, Portugal
    J Bioenerg Biomembr 33:343-52. 2001
    ..7. This behavior is consistent with the proposal that in these enzymes menaquinone reduction occurs close to heme bL, near to the periplasmic side of the membrane, and involving dissipation of the proton transmembrane gradient...
  11. doi request reprint The alternative complex III of Rhodothermus marinus and its structural and functional association with caa3 oxygen reductase
    Patricia N Refojo
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica, EAN, 2780 157 Oeiras, Portugal
    Biochim Biophys Acta 1797:1477-82. 2010
    ..This work is thus a step forward in the recognition of the structural and functional diversities of prokaryotic respiratory chains...
  12. pmc Redox properties of Thermus thermophilus ba3: different electron-proton coupling in oxygen reductases?
    Filipa L Sousa
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, 2781 901 Oeiras, Portugal
    Biophys J 94:2434-41. 2008
    ..4, the order is reversed: 246 mV for heme B and 199 mV for heme A3. The existence of redox anticooperativity was established by introducing a redox interaction parameter in a model of pairwise interacting redox centers...
  13. ncbi request reprint Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: phylogenetic relationships, metal centres and membrane attachment
    Rita S Lemos
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Oeiras, Portugal
    Biochim Biophys Acta 1553:158-70. 2002
    ..Finally, the possible contribution of these enzymes to the formation/dissipation of a transmembrane proton gradient is discussed, considering recent experimental and structural data...
  14. ncbi request reprint A ba3 oxygen reductase from the thermohalophilic bacterium Rhodothermus marinus
    Andreia F Veríssimo
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Oeiras, Portugal
    FEMS Microbiol Lett 269:41-7. 2007
    ..Both haems, B and A, present two transitions, have unusually low reduction potentials of -65 mV and an interaction potential of -52.5 mV...
  15. doi request reprint Energy conservation by Rhodothermus marinus respiratory complex I
    Ana P Batista
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica EAN, Oeiras, Portugal
    Biochim Biophys Acta 1797:509-15. 2010
    ....
  16. doi request reprint SERR-spectroelectrochemical study of a cbb3 oxygen reductase in a biomimetic construct
    Smilja Todorovic
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, EAN, 2780 157 Oeiras, Portugal
    J Phys Chem B 112:16952-9. 2008
    ..400 mV. The determination of reduction potentials of the individual hemes c reported in this work provides the basis for further exploring the mechanism of electroprotonic energy transduction of this complex enzyme...
  17. doi request reprint A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23 A resolution of rhodothermus marinus cytochrome c
    Meike Stelter
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, 2780 157 Oeiras, Portugal
    Biochemistry 47:11953-63. 2008
    ..Based on a thorough structural and amino acid sequence comparison, we propose R. marinus cytochrome c as the first characterized member of a new class of C-type cytochromes...
  18. ncbi request reprint Investigation of protonatable residues in Rhodothermus marinus caa3 haem-copper oxygen reductase: comparison with Paracoccus denitrificans aa3 haem-copper oxygen reductase
    Claudio M Soares
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Apartado 127, Av da Republica, 2781 901 Oeiras, Portugal
    J Biol Inorg Chem 9:124-34. 2004
    ..Two (Tyr262(I) and Lys336(I), caa(3) numbering) out of three protonatable K-channel residues are proton active and redox sensitive in both proteins...
  19. ncbi request reprint Thermodynamic redox behavior of the heme centers of cbb3 heme-copper oxygen reductase from Bradyrhizobium japonicum
    Andreia F Veríssimo
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Apartado 127, Av da Republica EAN, 2781 901 Oeiras, Portugal
    Biochemistry 46:13245-53. 2007
    ....
  20. ncbi request reprint A ferredoxin from the thermohalophilic bacterium Rhodothermus marinus
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Rua da Quinta, Grande 6, Apt 127, 2780 156 Oeiras, Portugal
    Biochim Biophys Acta 1601:1-8. 2002
    ..0 M GuHCl (pH 7.0, 20 degrees C). The iron-sulfur cluster degrades upon polypeptide unfolding, resulting in an irreversible denaturation process...
  21. ncbi request reprint Plasticity of proton pathways in haem-copper oxygen reductases
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780 156 Oeiras, Portugal
    FEBS Lett 522:14-8. 2002
    ..The diversity of channels in haem-copper oxygen reductases exemplifies the plasticity of proton pathways that occurred throughout evolution, and strongly suggests a substantial role for water as the main proton carrier...
  22. doi request reprint Proximal mutations at the type 1 copper site of CotA laccase: spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants
    Paulo Durão
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica, 2781 901 Oeiras, Portugal
    Biochem J 412:339-46. 2008
    ..The redox potentials of the L386A and I494A mutants are shifted downwards by approx. 60 and 100 mV respectively. These changes correlate well with decreased catalytic efficiency of both mutants compared with the wild-type...
  23. ncbi request reprint Quinone reduction by Rhodothermus marinus succinate:menaquinone oxidoreductase is not stimulated by the membrane potential
    Andreia S Fernandes
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica, Apartado 127, 2784 505 Oeiras, Portugal
    Biochem Biophys Res Commun 330:565-70. 2005
    ..The role of the membrane potential in regulation of the SQR activity is discussed...
  24. ncbi request reprint A nhaD Na+/H+ antiporter and a pcd homologues are among the Rhodothermus marinus complex I genes
    Ana M P Melo
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica, Apartado 127, 2781 901 Oeiras, Portugal
    Biochim Biophys Acta 1709:95-103. 2005
    ..Moreover, 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. The possible role of these two genes in R. marinus complex I is discussed...
  25. ncbi request reprint Midpoint potentials of hemes a and a3 in the quinol oxidase from Acidianus ambivalens are inverted
    Smilja Todorovic
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Apartado 127, 2781 901 Oeiras, Portugal
    J Am Chem Soc 127:13561-6. 2005
    ..These results suggest that the membrane potential may play an active role in the regulation of the enzymatic activity of QO...
  26. ncbi request reprint Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat
    Ligia O Martins
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica, 2781 901 Oeiras, Portugal
    J Biol Chem 277:18849-59. 2002
    ..Remarkably, the coat-associated or the purified enzyme showed a half-life of inactivation at 80 degrees C of about 4 and 2 h, respectively, indicating that CotA is intrinsically highly thermostable...
  27. ncbi request reprint Respiratory chains from aerobic thermophilic prokaryotes
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica, Apartado 127, 2781 901 Oeiras, Portugal
    J Bioenerg Biomembr 36:93-105. 2004
    ..Rather, the extensive genomic analyses indicate that the differences concerning the several complexes are related to the organism phylogeny, i.e., to evolution and lateral gene transfer events...
  28. ncbi request reprint A robust metallo-oxidase from the hyperthermophilic bacterium Aquifex aeolicus
    André T Fernandes
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Oeiras, Portugal
    FEBS J 274:2683-94. 2007
    ..McoA probably contributes to copper and iron homeostasis in A. aeolicus...
  29. ncbi request reprint Proton pathways, ligand binding and dynamics of the catalytic site in haem-copper oxygen reductases: a comparison between the three families
    Manuela M Pereira
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apt 127, 2780 156 Oeiras, Portugal
    Biochim Biophys Acta 1655:340-6. 2004
    ..Biophys. Acta 1505 (2001) 185], and allow to identify the minimal essential elements for these enzymes...
  30. ncbi request reprint Copper incorporation into recombinant CotA laccase from Bacillus subtilis: characterization of fully copper loaded enzymes
    Paulo Durão
    Universidade Nova de Lisboa, Av da Republica, 2781 901, Oeiras, Portugal
    J Biol Inorg Chem 13:183-93. 2008
    ..EPR and resonance Raman data indicate that, presumably, folding in the presence of copper is indispensable for the correct structure of the trinuclear copper-containing site...
  31. ncbi request reprint Purification and characterization of the complex I from the respiratory chain of Rhodothermus marinus
    Andreia S Fernandes
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780 156 Oeiras, Portugal
    J Bioenerg Biomembr 34:413-21. 2002
    ..At least five iron-sulfur centers are observed by EPR spectroscopy: two [2Fe-2S](2+/1+) and three [4Fe-4S](2+/1+) centers. By fluorescence spectroscopy a still unidentified chromophore was detected in R. marinus complex I...
  32. ncbi request reprint Electron paramagnetic resonance studies of the iron-sulfur centers from complex I of Rhodothermus marinus
    Andreia S Fernandes
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica, Apartado 127, 2784 505 Oeiras, Portugal
    Biochemistry 45:1002-8. 2006
    ..5...
  33. doi request reprint The cytochrome ba complex from the thermoacidophilic crenarchaeote Acidianus ambivalens is an analog of bc(1) complexes
    Tiago M Bandeiras
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica EAN, 2780 157 Oeiras, Portugal
    Biochim Biophys Acta 1787:37-45. 2009
    ..Based on these findings, we propose that the A. ambivalens cytochrome ba complex is analogous to the bc(1) complexes of bacteria and mitochondria, however with distinct subunits and heme types...
  34. doi request reprint Structural and functional insights into sulfide:quinone oxidoreductase
    José A Brito
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av da Republica EAN, 2780 157 Oeiras, Portugal
    Biochemistry 48:5613-22. 2009
    ..The possible implications of this observation in the catalytic mechanism for sulfide oxidation are discussed, and the role of SQR in the sulfur dependent bioenergetics of A. ambivalens, linked to oxygen reduction, is addressed...
  35. doi request reprint The dihydrolipoamide dehydrogenase from the crenarchaeon Acidianus ambivalens
    Ana P Batista
    Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Oeiras, Portugal
    FEMS Microbiol Lett 281:147-54. 2008
    ..Although DLDH is generally part of the alpha-ketoacid dehydrogenase complexes in Bacteria and Eukarya, none of these complexes has yet been isolated from Sulfolobales. The metabolic role of DLDH in these organisms is discussed...
  36. ncbi request reprint Structure at 1.3 A resolution of Rhodothermus marinus caa(3) cytochrome c domain
    Vasundara Srinivasan
    Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Marie Curie Str 15, D 60439 Frankfurt am Main, Germany
    J Mol Biol 345:1047-57. 2005
    ....
  37. ncbi request reprint Active site structure of the aa3 quinol oxidase of Acidianus ambivalens
    Tapan Kanti Das
    Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, USA
    Biochim Biophys Acta 1655:306-20. 2004
    ..The implications of such conformational changes are discussed in relation to general redox-coupled proton pumping mechanisms in the heme-copper oxygen reductases...