Publications

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Teixeira, L. R., J. M. Dantas, C. A. Salgueiro, and C. M. Cordas. "Thermodynamic and kinetic properties of the outer membrane cytochrome OmcF, a key protein for extracellular electron transfer in Geobacter sulfurreducens." Biochimica et Biophysica Acta - Bioenergetics. 1859.10 (2018): 1132-1137. AbstractWebsite
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Teixeira, L. R., C. M. Cordas, M. P. Fonseca, N. E. C. Duke, P. R. Pokkuluri, and C. A. Salgueiro. "Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducens." Frontiers in Microbiology. 10 (2020). AbstractWebsite
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Santos, T. C., A. R. De Oliveira, J. M. Dantas, C. A. Salgueiro, and C. M. Cordas. "Thermodynamic and kinetic characterization of PccH, a key protein in microbial electrosynthesis processes in Geobacter sulfurreducens." Biochimica et Biophysica Acta - Bioenergetics. 1847.10 (2015): 1113-1118. AbstractWebsite
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Samhan-Arias, A. K., S. Fortalezas, C. M. Cordas, I. Moura, JJG Moura, and C. Gutierrez-Merino. "Cytochrome b5 reductase is the component from neuronal synaptic plasma membrane vesicles that generates superoxide anion upon stimulation by cytochrome c." Redox Biology. 15 (2018): 109-114. AbstractWebsite
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Samhan-Arias, A. K., C. M. Cordas, M. S. Carepo, L. B. Maia, C. Gutierrez-Merino, I. Moura, and JJG Moura. "Ligand accessibility to heme cytochrome b 5 coordinating sphere and enzymatic activity enhancement upon tyrosine ionization." Journal of Biological Inorganic Chemistry. 24.3 (2019): 317-330. AbstractWebsite
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Samhan-Arias, A. K., R. M. Almeida, S. Ramos, C. M. Cordas, I. Moura, C. Gutierrez-Merino, and JJG Moura. "Topography of human cytochrome b5/cytochrome b5 reductase interacting domain and redox alterations upon complex formation." Biochimica et Biophysica Acta - Bioenergetics. 1859.2 (2018): 78-87. AbstractWebsite
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Samhan-Arias, A. K., L. B. Maia, C. M. Cordas, I. Moura, C. Gutierrez-Merino, and JJG Moura. "Peroxidase-like activity of cytochrome b5 is triggered upon hemichrome formation in alkaline pH." Biochimica et Biophysica Acta - Proteins and Proteomics. 1866.2 (2018): 373-378. AbstractWebsite
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Rosa, V., A. P. S. Gaspari, F. Folgosa, C. M. Cordas, P. Tavares, T. Santos-Silva, S. Barroso, and T. Avilés. "Imine ligands based on ferrocene: Synthesis, structural and Mössbauer characterization and evaluation as chromogenic and electrochemical sensors for Hg2+." New Journal of Chemistry. 42.5 (2018): 3334-3343. AbstractWebsite
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Rebocho, S., C. M. Cordas, R. Viveiros, and T. Casimiro. "Development of a ferrocenyl-based MIP in supercritical carbon dioxide: Towards an electrochemical sensor for bisphenol A." Journal of Supercritical Fluids. 135 (2018): 98-104. AbstractWebsite
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Ramos, S., R. M. Almeida, C. M. Cordas, JJG Moura, S. R. Pauleta, and I. Moura. "Insights into the recognition and electron transfer steps in nitric oxide reductase from Marinobacter hydrocarbonoclasticus." Journal of Inorganic Biochemistry. 177 (2017): 402-411. AbstractWebsite
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Ramanaiah, S. V., C. M. Cordas, S. Matias, and L. P. Fonseca. "In situ electrochemical characterization of a microbial fuel cell biocathode running on wastewater." Catalysts. 11.7 (2021). AbstractWebsite
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Nunes, M. J., C. M. Cordas, JJG Moura, J. P. Noronha, and L. C. Branco. "Screening of Potential Stress Biomarkers in Sweat Associated with Sports Training." Sports Medicine - Open. 7.1 (2021). AbstractWebsite
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Matias, S. C., N. M. T. Lourenço, L. J. P. Fonseca, and C. M. Cordas. "Comparative Electrochemical Behavior of Cytochrome c on Aqueous Solutions Containing Choline-Based Room Temperature Ionic Liquids." ChemistrySelect. 2.27 (2017): 8701-8705. AbstractWebsite
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Maiti, B. K., L. B. Maia, AJ Moro, J. C. Lima, C. M. Cordas, I. Moura, and JJG Moura. "Unusual Reduction Mechanism of Copper in Cysteine-Rich Environment." Inorganic Chemistry. 57.14 (2018): 8078-8088. AbstractWebsite
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Gomes, F. O., L. B. Maia, C. Cordas, C. Delerue-Matos, I. Moura, JJG Moura, and S. Morais. "Nitric Oxide Detection Using Electrochemical Third-generation Biosensors – Based on Heme Proteins and Porphyrins." Electroanalysis. 30.11 (2018): 2485-2503. AbstractWebsite
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Gomes, F. O., L. B. Maia, C. Cordas, I. Moura, C. Delerue-Matos, JJG Moura, and S. Morais. "Electroanalytical characterization of the direct Marinobacter hydrocarbonoclasticus nitric oxide reductase-catalysed nitric oxide and dioxygen reduction." Bioelectrochemistry. 125 (2019): 8-14. AbstractWebsite
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Folgosa, F., C. M. Cordas, J. A. Santos, AS Pereira, JJG Moura, P. Tavares, and I. Moura. "New spectroscopic and electrochemical insights on a class I superoxide reductase: evidence for an intramolecular electron-transfer pathway." Biochemical Journal. 438 (2011): 485-494. AbstractWebsite

SORs (superoxide reductases) are enzymes involved in bacterial resistance to reactive oxygen species, catalysing the reduction of superoxide anions to hydrogen peroxide. So far three structural classes have been identified. Class I enzymes have two ironcentre-containing domains. Most studies have focused on the catalytic iron site (centre II), yet the role of centre I is poorly understood. The possible roles of this iron site were approached by an integrated study using both classical and fast kinetic measurements, as well as direct electrochemistry. A new heterometallic form of the protein with a zinc-substituted centre I, maintaining the iron active-site centre II, was obtained, resulting in a stable derivative useful for comparison with the native all-iron from. Second-order rate constants for the electron transfer between reduced rubredoxin and the different SOR forms were determined to be 2.8 x 10(7) M(-1) . s(-1) and 1.3 x 10(6) M(-1) . s(-1) for SOR(Fe(IIII)-Fe(II)) and for SOR(Fe(IIII)-Fe(III)) forms respectively, and 3.2 x 10(6) M(-1) s(-1) for the SOR(Zn(II)-Fe(III)) form. The results obtained seem to indicate that centre I transfers electrons from the putative physiological donor rubredoxin to the catalytic active iron site (intramolecular process). In addition, electrochemical results show that conformational changes are associated with the redox state of centre I, which may enable a faster catalytic response towards superoxide anion. The apparent rate constants calculated for the SOR-mediated electron transfer also support this observation.

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Duarte, A. G., C. M. Cordas, JJG Moura, and I. Moura. "Steady-state kinetics with nitric oxide reductase (NOR): New considerations on substrate inhibition profile and catalytic mechanism." Biochimica et Biophysica Acta - Bioenergetics. 1837.3 (2014): 375-384. AbstractWebsite
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Dall'Agnol, L. T., C. M. Cordas, and JJG Moura. "Influence of respiratory substrate in carbon steel corrosion by a Sulphate Reducing Prokaryote model organism." Bioelectrochemistry. 97 (2014): 43-51. AbstractWebsite
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Cordas, C. M., N. M. T. Lourenco, P. Vidinha, CAM Afonso, S. Barreiros, L. P. Fonseca, and J. M. S. Cabral. "New conducting biomaterial based on Ion Jelly (R) technology for development of a new generation of biosensors." New Biotechnology. 25 (2009): S138-S139. AbstractWebsite
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Cordas, C. M., M. Campaniço, R. Baptista, L. B. Maia, I. Moura, and JJG Moura. "Direct electrochemical reduction of carbon dioxide by a molybdenum-containing formate dehydrogenase." Journal of Inorganic Biochemistry. 196 (2019). AbstractWebsite
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Cordas, Cristina M., Americo G. Duarte, Jose J. G. Moura, and Isabel Moura. "Electrochemical behaviour of bacterial nitric oxide reductase-Evidence of low redox potential non-heme Fe-B gives new perspectives on the catalytic mechanism." Biochimica Et Biophysica Acta-Bioenergetics. 1827.3 (2013): 233-238. Abstract
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Cordas, C. M., A. Tenreiro, and L. M. Abrantes EQCM study on the polytyramine modified electrodes for the preparation of biosensors. Eds. Y. G. Gogotsi, and I. V. Uvarova. Vol. 102. Nanostructured Materials and Coatings for Biomedical and Sensor Applications, 102., 2003. AbstractWebsite
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Cordas, C. M., I. Moura, and JJG Moura. "Direct electrochemical study of the multiple redox centers of hydrogenase from Desulfovibrio gigas." Bioelectrochemistry. 74.1 (2008): 83-89. AbstractWebsite

Direct electrochemical response was first time observed for the redox centers of Desulfovibrio gigas [NiFe]-Hase, in non-turnover conditions, by cyclic voltammetry, in solution at glassy carbon electrode. The activation of the enzyme was achieved by reduction with H(2) and by electrochemical control and electrocatalytic activity was observed. The inactivation of the [NiFe]-Hase was also attained through potential control. All electrochemical data was obtained in the absence of enzyme inhibitors. The results are discussed in the context of the proposed mechanism currently accepted for activation/inactivation of [NiFe]-Hases. (C) 2008 Elsevier B.V. All rights reserved.

Cordas, C. M., A. S. Viana, S. Leupold, F. P. Montforts, and L. M. Abrantes. "Self-assembled monolayer of an iron(III) porphyrin disulphide derivative on gold." Electrochemistry Communications. 5.1 (2003): 36-41. AbstractWebsite

A novel iron(III) porphyrin disulphide derivative have been successfully immobilised on gold surfaces by self-assembly. The redox response of the modified electrodes was compared with the obtained for a similar iron porphyrin in solution, confirming the immobilisation of the metalloporphyrin. The gravimetric data obtained by electrochemical quartz crystal microbalance (EQCM) during adsorption allowed an estimation of the electrode coverage, providing further evidence for the formation of the porphyrin SAM. The modified electrodes were also measured by conventional and imaging ellipsometry. The electrocatalytic activity of the two modified electrodes was tested for the reduction of the molecular oxygen. (C) 2002 Elsevier Science B.V. All rights reserved.