Publications

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2019
Ligand accessibility to heme cytochrome b5 coordinating sphere and enzymatic activity enhancement upon tyrosine ionization, Samhan-Arias, A. K., Cordas C. M., Carepo M. S., Maia L. B., Gutierrez-Merino C., Moura I., and Moura J. J. G. , J Biol Inorg Chem, Volume 24, p.317-330, (2019)
Molybdenum and tungsten enzymes: a brief overview, Cordas, C. M., and Moura J. J. G. , Coord Chem Rev, Volume 394, p.53-64, (2019)
NiII -ATCUN-catalyzed tyrosine nitration in the presence of nitrite and sulfite, Maiti, B. K., Maia L. B., Moura I., and Moura J. J. G. , Chem Eur J, Volume 25, p.4309-4314, (2019) Website
Source and reduction of nitrous oxide, Pauleta, S. R., Carepo M. S., and Moura I. , Coord Chem Rev, Volume 387, p.436-449, (2019)
Third-generation electrochemical biosensor based on nitric oxide reductase immobilized in a multiwalled carbon nanotubes/1-n-butyl-3-methylimidazolium tetrafluoroborate nanocomposite for nitric oxide detection, Gomes, FO, Maia L. B., Delerue-Matos C., Moura I., Moura J. J. G., and Morais S. , Sensors & Actuators: B. Chemical, Volume 285, p.445-452, (2019) Website
The treta copper-sulfide center of nitrous oxide reductase, Pauleta, S. R., Carepo M. S., and Moura I. , Transition Metals and Sulfur- A Strong Relationship with Life, Berlin, p.Chapter 5, (2019)
2018
Cytochrome b5 reductase is the component from neuronal synaptic plasma membrane vesicles that generates superoxide anion upon stimulation by cytochrome c, Samhan-Arias, A. K., Fortalezas S., Cordas C., Moura I., Moura J. J. G., and Gutierrez-Merino C. , Redox Biol, Volume 15, p.109-114, (2018)
Development of a ferrocenyl-based MIP in supercritical carbon dioxide: Towards an electrochemical sensor for bisphenol A, Rebocho, S., Cordas C. M., Viveiros R., and Casimiro T. , J Supercrit Fluids, Volume 135, p.98-104, (2018) Website
Genomic organization, gene expression and activity profile of Marinobacter hydrocarbonoclasticus denitrification enzymes, Carreira, C., Mestre O., Nunes R. F., Moura I., and Pauleta S. R. , PEERJ, Volume 6, p.DOI: 10.7717/peerj.5603, (2018)
Imine Ligands Based on Ferrocene: Synthesis, Structural and Mössbauer Characterization and Evaluation as Chromogenic and Electrochemical Sensors for Hg+2, Rosa, V., Gaspari A., Folgosa F., Cordas C. M., Tavares P., Santos-Silva T., Barroso S., and Avilés T. , New J Chem, Volume 42, p.3334-3343, (2018) Website
Mononuclear molybdenum-containing enzymes, Maia, L., and Moura J. J. G. , Reference Module in Chemistry, Volume Molecular Sciences and Chemical Engineering, p.1 - 19, (2018) Website
Nitric oxide detection using electrochemical third-generation biosensors – based on heme proteins and porphyrins, Gomes, F., Maia L., Cordas C., Delerue-Matos C., Moura I., Moura J. J. G., and Morais S. , Electroanalysis, Volume 30, p.1-20, (2018) Website
Peroxidase-like activity of cytochrome b5 is triggered upon hemichrome formation in alkaline pH, Samhan-Arias, A., Maia L. B., Cordas C. M., Moura I., Gutierrez-Merino C., and Moura J. J. G. , BBA - Proteins and Proteomics, Volume 1866, p.373-378, (2018)
Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: nitrite reduction by molybdoenzymes, Maia, L., and Moura J. J. G. , Redox Biol, Volume 19, p.274-289, (2018) redoxbiol-2018-19-274.pdfWebsite
Small phospho-donors phosphorylate MorR without inducing protein conformational changes, Castro, N. S. S., Laia C. A. T., Maiti B. K., Cerqueira N., Moura I., and Carepo M. S. P. , Biophys Chem, Volume 240, p.25-33, (2018)
Thermodynamic and kinetic properties of the outer membrane cytochrome OmcF, a key protein for extracellular electron transfer in Geobacter sulfurreducens, Teixeira, L. R., Dantas J. M., Salgueiro C. A., and Cordas C. M. , BBA - Bioenergetics, Volume 1859, p.1132-1137, (2018) Website
Topography of human cytochrome b5/cytochrome b5 reductase interacting domain and redox alterations upon complex formation, Samhan-Arias, A. K., Almeida R. M., Ramos S., Cordas C. M., Moura I., Gutierrez-Merino C., and Moura J. J. G. , Biochim Biophys Acta, Volume 1859, p.78-87, (2018)
Unusual reduction mechanism of copper in cysteine-rich environment, Maiti, B. K., Maia L., Moro A. J., Lima J. C., Cordas C., Moura I., and Moura J. J. G. , Inorg Chem, Volume 57, p.8078-8088, (2018) Website
2017
A bird’s-eye view of denitrification in relation to the nitrogen cycle, Moura, I., Maia L. B., Pauleta S. R., and Moura J. J. G. , Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2)., Cambridge, p.1-10, (2017) n_cycle-rsc_book-denitrification-chap_1.pdf
The catalytic cycle of nitrous oxide reductase - The enzyme that catalyzes the last step of denitrification, Carreira, C., Pauleta S. R., and Moura I. , J Inorg Biochem, Volume 177, p.423-434, (2017)
Comparative electrochemical behavior of cytochrome c on aqueous solutions containing choline-based room temperature ionic liquids, Matias, S. C., Lourenço N. M. T., Fonseca J. P., and Cordas C. M. , ChemistrySelect, Volume 2, p.8701–8705, (2017) Website
Electron transfer and molecular recognition in denitrification and nitrate dissimilatory pathways, Almeida, R. M., Dell'Acqua S., Moura I., Pauleta S. R., and Moura J. J. G. , Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2)., p.252-286, (2017)
EPR spectroscopy on mononuclear molybdenum-containing enzymes, Maia, L. B., Moura I., and Moura J. J. G. , Future Directions in Metalloprotein and Metalloenzyme Research, Biological Magnetic Resonance, Vol. 33 (ISBN: 978-3-319-59100-1), Cham, p.55-101, (2017) Abstract

The biological relevance of molybdenum was demonstrated in the early 1950s-1960s, by Bray, Beinert, Lowe, Massey, Palmer, Ehrenberg, Pettersson, Vänngård, Hanson and others, with ground-breaking studies performed, precisely, by electron paramagnetic resonance (EPR) spectroscopy. Those earlier studies, aimed to investigate the mammalian xanthine oxidase and avian sulfite oxidase enzymes, demonstrated the surprising biological reduction of molybdenum to the paramagnetic Mo5+. Since then, EPR spectroscopy, alongside with other spectroscopic methods and X-ray crystallography, has contributed to our present detailed knowledge about the active site structures, catalytic mechanisms and structure/activity relationships of the molybdenum-containing enzymes.
This Chapter will provide a perspective on the contribution that EPR spectroscopy has made to some selected systems. After a brief overview on molybdoenzymes, the Chapter will be focused on the EPR studies of mammalian xanthine oxidase, with a brief account on the prokaryotic aldehyde oxidoreductase, nicotinate dehydrogenase and carbon monoxide dehydrogenase, vertebrate sulfite oxidase, and prokaryotic formate dehydrogenases and nitrate reductases.

Insights into nitrous oxide reductase, Pauleta, S. R., Carreira C., and Moura I. , Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2)., p.141-169, (2017)
Insights into the molybdenum/copper heterometallic cluster assembly in the orange protein: probing intermolecular interactions with an artificial metal-binding ATCUN tag, Maiti, B. K., Almeida R. M., Maia L. B., Moura I., and Moura J. J. G. , Inorg Chem, Volume 56, p.8900-8911, (2017) Website