Publications

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2019
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)
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)
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)
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
Insights into the recognition and electron transfer steps in nitric oxide reductase from Marinobacter hydrocarbonoclasticus, Ramos, S., Almeida R. M., Cordas C. M., Moura J. J. G., Pauleta S. R., and Moura I. , J Inorg Biochem, Volume 177, p.402-411, (2017)
Large core-shell affinity beads for gravity-driven API purification processes: A green strategy by molecular imprinting in supercritical CO2, Viveiros, R., Dias F. M., Maia L. B., Heggie W., and Casimiro T. , J Ind Eng Chem, Volume 54, p.341-349, (2017) Website
Lessons from denitrification to the human metabolism of signalling nitric oxide, Maia, L. B., and Moura J. J. G. , Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2)., p.419-443, (2017)
Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2)., Moura, I., Moura J. J. G., Pauleta S. R., and Maia L. B. , (2017) Website
Molybdenum and tungsten-containing enzymes: an overview, Maia, L. B., Moura I., and Moura J. J. G. , Molybdenum and Tungsten Enzymes: Biochemistry, RSC Metallobiology Series No. 5 (ISBN: 978-1-78262-089-1). , p.1-80, (2017) mo_w_enzymes-rsc_book_biochemistry-chap_1.pdf
Molybdenum and tungsten-containing formate dehydrogenases: aiming to inspire a catalyst for carbon dioxide utilization, Maia, L. B., Moura I., and Moura J. J. G. , Inorg Chim Acta, Volume 455, p.350-363, (2017)
application/pdf iconica-2017-455-350-free_until_2017-02-05.pdf
Website
Protein-Assisted Formation of Molybdenum Heterometallic Clusters: Evidence for the Formation of S2MoS2−M−S2MoS2 Clusters with M = Fe, Co, Ni, Cu, or Cd within the Orange Protein, Maiti, B. K., Maia L. B., Pauleta S. R., Moura I., and Moura J. J. G. , Inorg Chem, Volume 56, p.2210−2220, (2017) Website
Rubredoxins derivatives: Simple sulphur-rich coordination metal sites and its relevance for Biology and Chemistry, Maiti, B. K., Almeida R. M., Moura I., and Moura J. J. G. , Coord Chem Rev, Volume 352, p.379-397, (2017)