@article {15419, title = {In situ electrochemical characterization of a microbial fuel cell biocathode running on wastewater}, journal = {Catalysts}, volume = {11}, year = {2021}, note = {

Export Date: 22 September 2021

}, month = {2021}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85109407021\&doi=10.3390\%2fcatal11070839\&partnerID=40\&md5=5f1e7eb71e023065b73099213d388284}, author = {Ramanaiah, S.V. and Cordas, C. M. and Matias, S. and Fonseca, L. P.} } @article {15418, title = {Screening of Potential Stress Biomarkers in Sweat Associated with Sports Training}, journal = {Sports Medicine - Open}, volume = {7}, year = {2021}, note = {

Export Date: 22 September 2021

}, month = {2021}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85099737701\&doi=10.1186\%2fs40798-020-00294-3\&partnerID=40\&md5=c1f482b43cf061991222a74dc7809130}, author = {Nunes, M.J. and Cordas, C. M. and Moura, JJG and Noronha, J. P. and Branco, L.C.} } @article {15422, title = {Direct electrochemical reduction of carbon dioxide by a molybdenum-containing formate dehydrogenase}, journal = {Journal of Inorganic Biochemistry}, volume = {196}, year = {2019}, note = {

Cited By :8Export Date: 22 September 2021

}, month = {2019}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85064329089\&doi=10.1016\%2fj.jinorgbio.2019.110694\&partnerID=40\&md5=50c432c29bb7848be147db8cea806dee}, author = {Cordas, C. M. and M. Campani{\c c}o and R. Baptista and Maia, L. B. and Moura, I and Moura, JJG} } @article {15424, title = {Electroanalytical characterization of the direct Marinobacter hydrocarbonoclasticus nitric oxide reductase-catalysed nitric oxide and dioxygen reduction}, journal = {Bioelectrochemistry}, volume = {125}, year = {2019}, note = {

Cited By :3Export Date: 22 September 2021

}, month = {2019}, pages = {8 - 14}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85052882408\&doi=10.1016\%2fj.bioelechem.2018.08.005\&partnerID=40\&md5=e55a9f26bcc3227af5410e65be094a3d}, author = {Gomes, F.O. and Maia, L. B. and Cordas, C and Moura, I and C Delerue-Matos and Moura, JJG and S Morais} } @article {15423, title = {Ligand accessibility to heme cytochrome b 5 coordinating sphere and enzymatic activity enhancement upon tyrosine ionization}, journal = {Journal of Biological Inorganic Chemistry}, volume = {24}, year = {2019}, note = {

Cited By :1Export Date: 22 September 2021

}, month = {2019}, pages = {317 - 330}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85062720207\&doi=10.1007\%2fs00775-019-01649-2\&partnerID=40\&md5=8205ef2448bdd48e7af6c2c17d6c49cd}, author = {Samhan-Arias, A.K. and Cordas, C. M. and Carepo, M. S. and Maia, L. B. and C Gutierrez-Merino and Moura, I and Moura, JJG} } @article {15421, title = {Molybdenum and tungsten enzymes redox properties {\textendash} A brief overview}, journal = {Coordination Chemistry Reviews}, volume = {394}, year = {2019}, note = {

Cited By :9Export Date: 22 September 2021

}, month = {2019}, pages = {53 - 64}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85066260970\&doi=10.1016\%2fj.ccr.2019.05.005\&partnerID=40\&md5=6e01a4f19e971f3ee6fc8e14ea453317}, author = {Cordas, C. M. and Moura, JJG} } @article {15429, title = {Cytochrome b5 reductase is the component from neuronal synaptic plasma membrane vesicles that generates superoxide anion upon stimulation by cytochrome c}, journal = {Redox Biology}, volume = {15}, year = {2018}, note = {

Cited By :6Export Date: 22 September 2021

}, month = {2018}, pages = {109 - 114}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85037688715\&doi=10.1016\%2fj.redox.2017.11.021\&partnerID=40\&md5=5a8984abce7cace533ae58d764843022}, author = {Samhan-Arias, A.K. and Fortalezas, S. and Cordas, C. M. and Moura, I and Moura, JJG and C Gutierrez-Merino} } @article {15425, title = {Nitric Oxide Detection Using Electrochemical Third-generation Biosensors {\textendash} Based on Heme Proteins and Porphyrins}, journal = {Electroanalysis}, volume = {30}, year = {2018}, note = {

Cited By :6Export Date: 22 September 2021

}, month = {2018}, pages = {2485 - 2503}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85053027815\&doi=10.1002\%2felan.201800421\&partnerID=40\&md5=3243ea8943b21b1ac3f0238451254468}, author = {Gomes, F.O. and Maia, L. B. and Cordas, C and C Delerue-Matos and Moura, I and Moura, JJG and S Morais} } @article {15431, title = {Peroxidase-like activity of cytochrome b5 is triggered upon hemichrome formation in alkaline pH}, journal = {Biochimica et Biophysica Acta - Proteins and Proteomics}, volume = {1866}, year = {2018}, note = {

Cited By :3Export Date: 22 September 2021

}, month = {2018}, pages = {373 - 378}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85032274511\&doi=10.1016\%2fj.bbapap.2017.09.010\&partnerID=40\&md5=9abb5237293285f90c66fd82a7950832}, author = {Samhan-Arias, A.K. and Maia, L. B. and Cordas, C. M. and Moura, I and C Gutierrez-Merino and Moura, JJG} } @article {15430, title = {Topography of human cytochrome b5/cytochrome b5 reductase interacting domain and redox alterations upon complex formation}, journal = {Biochimica et Biophysica Acta - Bioenergetics}, volume = {1859}, year = {2018}, note = {

Cited By :6Export Date: 22 September 2021

}, month = {2018}, pages = {78 - 87}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85034043564\&doi=10.1016\%2fj.bbabio.2017.10.005\&partnerID=40\&md5=9484f49b2db5a0b358456664c7ab9b87}, author = {Samhan-Arias, A.K. and Almeida, R. M. and Ramos, S. and Cordas, C. M. and Moura, I and C Gutierrez-Merino and Moura, JJG} } @article {15427, title = {Unusual Reduction Mechanism of Copper in Cysteine-Rich Environment}, journal = {Inorganic Chemistry}, volume = {57}, year = {2018}, note = {

Cited By :6Export Date: 22 September 2021

}, month = {2018}, pages = {8078 - 8088}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85049995536\&doi=10.1021\%2facs.inorgchem.8b00121\&partnerID=40\&md5=39008292aa60a993a0f49e346e09a089}, author = {Maiti, B. K. and Maia, L. B. and AJ Moro and Lima, J.C. and Cordas, C. M. and Moura, I and Moura, JJG} } @article {15434, title = {Comparative Electrochemical Behavior of Cytochrome c on Aqueous Solutions Containing Choline-Based Room Temperature Ionic Liquids}, journal = {ChemistrySelect}, volume = {2}, year = {2017}, note = {

Cited By :4Export Date: 22 September 2021

}, month = {2017}, pages = {8701 - 8705}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85041810115\&doi=10.1002\%2fslct.201702052\&partnerID=40\&md5=af5d9a976b667530903f12a4df6acf62}, author = {Matias, S.C. and N. M. T. Louren{\c c}o and Fonseca, L.J.P. and Cordas, C. M.} } @article {15433, title = {Insights into the recognition and electron transfer steps in nitric oxide reductase from Marinobacter hydrocarbonoclasticus}, journal = {Journal of Inorganic Biochemistry}, volume = {177}, year = {2017}, note = {

Cited By :10Export Date: 22 September 2021

}, month = {2017}, pages = {402 - 411}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85029632658\&doi=10.1016\%2fj.jinorgbio.2017.09.001\&partnerID=40\&md5=9a4eded9a520a6b86683c937bb0f1889}, author = {Ramos, S. and Almeida, R. M. and Cordas, C. M. and Moura, JJG and Pauleta, S. R. and Moura, I} } @article {15435, title = {Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly}, journal = {ChemistrySelect}, volume = {1}, year = {2016}, note = {

Cited By :2Export Date: 22 September 2021

}, month = {2016}, pages = {6546 - 6552}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85041795531\&doi=10.1002\%2fslct.201601640\&partnerID=40\&md5=45cb271a56305e102702f5050c04f33f}, author = {Carvalho, R.N.L. and Almeida, R. M. and Moura, JJG and Louren{\c c}o, N.T. and Fonseca, L.J.P. and Cordas, C. M.} } @article {15438, title = {Influence of respiratory substrate in carbon steel corrosion by a Sulphate Reducing Prokaryote model organism}, journal = {Bioelectrochemistry}, volume = {97}, year = {2014}, note = {

Cited By :28Export Date: 22 September 2021

}, month = {2014}, pages = {43 - 51}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84895927474\&doi=10.1016\%2fj.bioelechem.2013.10.006\&partnerID=40\&md5=31c86a418b4c2ac9713493b86bd71312}, author = {Dall{\textquoteright}Agnol, L.T. and Cordas, C. M. and Moura, JJG} } @article {15437, title = {Steady-state kinetics with nitric oxide reductase (NOR): New considerations on substrate inhibition profile and catalytic mechanism}, journal = {Biochimica et Biophysica Acta - Bioenergetics}, volume = {1837}, year = {2014}, note = {

Cited By :26Export Date: 22 September 2021

}, month = {2014}, pages = {375 - 384}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84892396381\&doi=10.1016\%2fj.bbabio.2014.01.001\&partnerID=40\&md5=4305287449ca52f9d5c68f2c6909805e}, author = {Duarte, A. G. and Cordas, C. M. and Moura, JJG and Moura, I} } @article {4508, title = {Electrochemical behaviour of bacterial nitric oxide reductase-Evidence of low redox potential non-heme Fe-B gives new perspectives on the catalytic mechanism}, journal = {Biochimica Et Biophysica Acta-Bioenergetics}, volume = {1827}, year = {2013}, note = {n/a}, month = {MAR 2013}, pages = {233-238}, abstract = {n/a}, isbn = {0005-2728}, doi = {10.1016/j.bbabio.2012.10.018}, author = {Cordas, Cristina M and Duarte, Americo G and Moura, Jose J. G. and Moura, Isabel} } @article {15440, title = {Electrochemical behaviour of bacterial nitric oxide reductase - Evidence of low redox potential non-heme FeB gives new perspectives on the catalytic mechanism}, journal = {Biochimica et Biophysica Acta - Bioenergetics}, volume = {1827}, year = {2013}, note = {

Cited By :26Export Date: 22 September 2021

}, month = {2013}, pages = {233 - 238}, abstract = {n/a}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84871853154\&doi=10.1016\%2fj.bbabio.2012.10.018\&partnerID=40\&md5=d00e5800cdac49258051a823ff49eccb}, author = {Cordas, C. M. and Duarte, A. G. and Moura, JJG and Moura, I} } @article {4504, title = {Comparative electrochemical study of superoxide reductases}, journal = {European Biophysics Journal with Biophysics Letters}, volume = {41}, year = {2012}, note = {

Cordas, Cristina M. Raleiras, Patricia Auchere, Francoise Moura, Isabel Moura, Jose J. G.

}, month = {Feb}, pages = {209-215}, abstract = {

Superoxide reductases are involved in relevant biological electron transfer reactions related to protection against oxidative stress caused by reactive oxygen species. The electrochemical features of metalloproteins belonging to the three different classes of enzymes were studied by potentio-dynamic techniques (cyclic and square wave voltammetry): desulfoferrodoxin from Desulfovibrio vulgaris Hildenborough, class I superoxide reductases and neelaredoxin from Desulfovibrio gigas and Treponema pallidum, namely class II and III superoxide reductases, respectively. In addition, a small protein, designated desulforedoxin from D. gigas, which has high homology with the N-terminal domain of class I superoxide reductases, was also investigated. A comparison of the redox potentials and redox behavior of all the proteins is presented, and the results show that SOR center II is thermodynamically more stable than similar centers in different proteins, which may be related to an intramolecular electron transfer function.

}, isbn = {0175-7571}, doi = {10.1007/s00249-011-0777-1}, url = {://WOS:000299751600008}, author = {Cordas, C. M. and Raleiras, P and Auchere, F and Moura, I and Moura, JJG} } @article {4509, title = {New spectroscopic and electrochemical insights on a class I superoxide reductase: evidence for an intramolecular electron-transfer pathway}, journal = {Biochemical Journal}, volume = {438}, year = {2011}, note = {

Folgosa, Filipe Cordas, Cristina M. Santos, Joana A. Pereira, Alice S. Moura, Jose J. G. Tavares, Pedro Moura, IsabelPart 3

}, month = {Sep}, pages = {485-494}, abstract = {

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.

}, isbn = {0264-6021}, doi = {10.1042/bj20110836}, url = {://WOS:000295182100010}, author = {Folgosa, F and Cordas, C. M. and Santos, J. A. and Pereira, AS and Moura, JJG and Tavares, P. and Moura, I} } @article {4502, title = {Direct electrochemical study of the multiple redox centers of hydrogenase from Desulfovibrio gigas}, journal = {Bioelectrochemistry}, volume = {74}, year = {2008}, note = {

Cordas, Cristina M. Moura, Isabel Moura, Jose J. G.SI

}, month = {Nov}, pages = {83-89}, abstract = {

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.

}, isbn = {1567-5394}, doi = {10.1016/j.bioelechem.2008.04.019}, url = {://WOS:000261314000016}, author = {Cordas, C. M. and Moura, I and Moura, JJG} } @article {4500, title = {Electroactive biofilms of sulphate reducing bacteria}, journal = {Electrochimica Acta}, volume = {54}, year = {2008}, note = {

Cordas, Cristina M. Guerra, L. Tiago Xavier, Catarina Moura, Jose J. G.International Conference on Biocorrosion of MaterialsJUN 14-17, 2007Paris, FRANCESI

}, month = {Dec}, pages = {29-34}, abstract = {

Biofilms formed from a pure strain of Desulfovibrio desulfuricans 27774 on stainless steel and graphite polarised surfaces were studied. The polarisation conditions applied were -0.4V vs. SCE for different times. A cathodic current related with the biofilms growth was observed with a maximum intensity of -270 mA m(-2) that remained stable for several days using graphite electrodes. These sulphate reducing bacteria biofilms present electrocatalytic activity towards hydrogen and oxygen reduction reactions. Electrode polarisation has a selective effect on the catalytic activity. The biofilms were also observed by scanning electronic microscopy revealing the formation of homogeneous films on the surfaces. (c) 2008 Elsevier Ltd. All rights reserved.

}, isbn = {0013-4686}, doi = {10.1016/j.electacta.2008.02.041}, url = {://WOS:000260729900006}, author = {Cordas, C. M. and Guerra, L. T. and Xavier, C. and Moura, JJG} } @article {4503, title = {Nitric oxide reductase: Direct electrochemistry and electrocatalytic activity}, journal = {Chembiochem}, volume = {7}, year = {2006}, note = {

Cordas, Cristina M. Pereira, Alice S. Martins, Carlos E. Timoteo, Cristina G. Moura, Isabel Moura, Jose J. G. Tavares, Pedro

}, month = {Dec}, pages = {1878-1881}, abstract = {n/a}, isbn = {1439-4227}, doi = {10.1002/cbic.200600253}, url = {://WOS:000242981500009}, author = {Cordas, C. M. and Pereira, AS and Martins, C. E. and Timoteo, C. G. and Moura, I and Moura, JJG and Tavares, P.} } @article {4499, title = {Overexpression and purification of Treponema pallidum rubredoxin; kinetic evidence for a superoxide-mediated electron transfer with the superoxide reductase neelaredoxin}, journal = {Journal of Biological Inorganic Chemistry}, volume = {9}, year = {2004}, note = {n/a}, month = {OCT 2004}, pages = {839-849}, abstract = {n/a}, doi = {10.1007/s00775-004-0584-6}, author = {Auchere, F and Sikkink, R and Cordas, C and Raleiras, P and Tavares, P. and Moura, I and Moura, JJG} } @article {4506, title = {Self-assembled monolayer of an iron(III) porphyrin disulphide derivative on gold}, journal = {Electrochemistry Communications}, volume = {5}, year = {2003}, note = {

Cordas, CM Viana, AS Leupold, S Montforts, FP Abrantes, LM

}, month = {Jan}, pages = {36-41}, abstract = {

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.

}, isbn = {1388-2481}, doi = {10.1016/s1388-2481(02)00530-1}, url = {://WOS:000180434200008}, author = {Cordas, C. M. and Viana, A. S. and Leupold, S. and Montforts, F. P. and Abrantes, L. M.} }