T
Teresa Catarino
Researcher at Universidade Nova de Lisboa
Publications - 39
Citations - 1010
Teresa Catarino is an academic researcher from Universidade Nova de Lisboa. The author has contributed to research in topics: Geobacter sulfurreducens & Cytochrome. The author has an hindex of 18, co-authored 35 publications receiving 936 citations. Previous affiliations of Teresa Catarino include Faculdade de Ciências e Tecnologia da Universidade Nova de Lisboa & University of Georgia.
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Journal ArticleDOI
NMR Studies of Cooperativity in the Tetrahaem Cytochrome c3 from Desulfovibrio vulgaris
David L. Turner,David L. Turner,Carlos A. Salgueiro,Teresa Catarino,Jean LeGall,Jean LeGall,António V. Xavier +6 more
TL;DR: Comparison with the crystal structure together with measurement of the kinetics of proton exchange suggest that the pH dependence is mediated by a charged residue(s) readily acessible to the solvent and close to haem I.
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Structures and solution properties of two novel periplasmic sensor domains with c-type heme from chemotaxis proteins of Geobacter sulfurreducens: implications for signal transduction.
P.R. Pokkuluri,Miguel Pessanha,Yuri Y. Londer,S. J. Wood,N. E. C. Duke,Robert Wilton,Teresa Catarino,Teresa Catarino,Carlos A. Salgueiro,Marianne Schiffer +9 more
TL;DR: Optical absorption, electron paramagnetic resonance and NMR spectroscopy have revealed that the heme groups of both sensor domains are high-spin and low-spin in the oxidized and reduced forms, respectively, and that the spin-state interconversion involves a heme axial ligand replacement.
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Redox-Bohr effect in electron/proton energy transduction: cytochrome c 3 coupled to hydrogenase works as a 'proton thruster' in Desulfovibrio vulgaris
TL;DR: This mechanism, which requires a relocation of the proposed proton channel in the hydrogenase structure, is similar to that proposed for the transmembrane proton pumps, and is the first example which shows evidence of functional energy transduction in the absence of a membrane confinement.
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Cooperativity between electrons and protons in a monomeric Cytochrome c3: the importance of mechano-chemical coupling for energy transduction
TL;DR: The microscopic characterisation allows the identification of several pairs of centres for which there are clear conformational (non‐Coulombic) contributions to their coupling energies, thus establishing the existence of localised redox‐ and acid–base‐linked structural modifications in the protein (mechano‐chemical coupling).
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Functional and Mechanistic Studies of Cytochrome c3 from Desulfovibrio gigas: Thermodynamics of a “Proton Thruster” †
Ricardo O. Louro,Teresa Catarino,D.L. Turner,M.A Piçarra-Pereira,Pacheco I,Jean LeGall,Xavier Av +6 more
TL;DR: The network of interactions between the centers in this protein facilitates the concerted transfer of electrons and protons, in agreement with the "proton thruster" mechanism proposed for electronic to protonic energy transduction by cytochromes c3.