publications

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2019
Gomes F, Maia L, Loureiro JA, Pereira MC, Delerue-Matos C, Moura I, Moura JJG, Morais S. "Biosensor for direct bioelectrocatalysis detection of nitric oxide using nitric oxide reductase incorporated in carboxylated single-walled carbon nanotubes/lipidic 3 bilayer nanocomposite." Bioelectrochem. 2019;127:76-86. AbstractWebsite

https://docentes.fct.unl.pt/lblm/files/bioelectrochem-2019-127-76.pdf

Cordas C, Campaniço M, Baptista R, Maia L, Moura I, Moura JJG. "Direct electrochemical reduction of carbon dioxide by a molybdenum-containing formate dehydrogenase." J Inorg Biochem. 2019;196:110694. AbstractWebsite

https://docentes.fct.unl.pt/lblm/files/jib-2019-196-110694.pdf

Gomes F, Maia L, Cordas C, Moura I, Delerue-Matos C, Moura JJG, Morais S. "Electroanalytical characterization of the direct Marinobacter hydrocarbonoclasticus nitric oxide reductase-catalysed nitric oxide and dioxygen reduction." Bioelectrochem. 2019;125:8-14. AbstractWebsite

https://docentes.fct.unl.pt/lblm/files/bioelectrochem-2019-125-8.pdf

Maiti BK, Maia L, Moura I, Moura JJG. "NiII-ATCUN-catalyzed tyrosine nitration in the presence of nitrite and sulfite." Chem Eur J. 2019;25:4309-4314. AbstractWebsite

https://docentes.fct.unl.pt/lblm/files/chemeurj-2019-25-4309.pdf

Gomes F, Maia L, Delerue-Matos C, Moura I, Moura JJG, Morais S. "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." Sensors Act B Chem. 2019;285:445-452. AbstractWebsite

https://docentes.fct.unl.pt/lblm/files/sensorsactbchem-2019-285-445.pdf

2018
Maia LB, Moura JJG. "Mononuclear molybdenum-containing enzymes.". In: Reference Module in Chemistry, Molecular Sciences and Chemical Engineering. Elsevier; 2018:. Abstract

https://docentes.fct.unl.pt/lblm/files/refmodchem-2018---1.pdf

Gomes F, Maia L, Cordas C, Delerue-Matos C, Moura I, Moura JJG, Morais S. "Nitric oxide detection using electrochemical third-generation biosensors – based on heme proteins and porphyrins." Electroanalysis. 2018;30:2485-2503. AbstractWebsite

https://docentes.fct.unl.pt/lblm/files/electroanalysis-2018-30-2485.pdf

Samhan-Arias A, Maia L, Cordas CM, Moura I, Gutierrez-Merino C, Moura JJG. "Peroxidase-like activity of cytochrome b5 is triggered upon hemichrome formation in alkaline pH." BBA - Proteins and Proteomics. 2018;1866:373-378. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/bba-2018-1866-373.pdf

Maia LB, Moura JJG. "Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: nitrite reduction by molybdoenzymes." Redox Biol. 2018;19:274-289. Abstract
application/pdf icon_Redox_Biol-2018-19-274.pdf
Website

https://docentes.fct.unl.pt/lblm/files/redoxbiol-2018-19-274.pdf

Maiti BK, Maia L, Moro AJ, Lima JC, Cordas CM, Moura I, Moura JJG. "Unusual reduction mechanism of copper in cysteine-rich environment." Inorg Chem. 2018;57:8078-8088. AbstractWebsite

https://docentes.fct.unl.pt/lblm/files/inorgchem-2018-57-8078.pdf

2017
Moura I, Maia LB, Pauleta SR, Moura JJG. "A bird’s-eye view of denitrification in relation to the nitrogen cycle." In: Moura I, Moura JJG, Pauleta SR, Maia LB, eds. Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2). Vol. 39. The Royal Society of Chemistry; 2017:. Abstract
application/pdf icon_RSC_Book-Denitrification-2017-Chap_1.pdf

This book is devoted to denitrification, an anaerobic process that is used by a wide range of bacteria for energy generation. The overall process involves nitrate, which is present in soil or water, being reduced to gaseous dinitrogen. This initial chapter aims to place denitrification in the larger context of the nitrogen biogeochemical cycle (a bird’s eye view). Detailed topics are developed through the many following contributions. Denitrification is a landscape for probing the structures, functions and mechanisms of action of a wide range of highly specialised metalloenzymes. These carry out, sequentially, four oxo-transfer reactions: NO3− → NO2− → ˙NO → N2O → N2. The environmental implications of these processes are of particular relevance. Nitrate accumulation and the release of nitrous oxide into the atmosphere due to the excessive use of fertilisers in agriculture are examples of two environmental problems in which denitrification plays a central role.

http://docentes.fct.unl.pt/lblm/files/rsc_book-denitrification-2017-chap_1.pdf

Maia LB, Moura I, Moura JJG. "EPR spectroscopy on mononuclear molybdenum-containing enzymes." In: Hanson G, Berliner LJ, eds. Future Directions in Metalloprotein and Metalloenzyme Research, Biological Magnetic Resonance, Vol. 33 (ISBN: 978-3-319-59100-1). Vol. 12. Cham: Springer Publishers; 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.

http://docentes.fct.unl.pt/lblm/files/epr_book-chap_4.pdf

Viveiros R, Dias FM, Maia L, Heggie W, Casimiro T. "Green strategy to produce large core-shell affinity beads for gravity-driven API purification processes." J Ind Eng Chem. 2017;54:341-349. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/jiengchem-2017-54-341.pdf

Maiti BK, Almeida RM, Maia L, Moura I, Mura JJG. "Insights into the molybdenum/copper heterometallic cluster assembly in the orange protein: probing intermolecular interactions with an artificial metal-binding ATCUN tag." Inorg Chem. 2017;56: 8900-8911. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/inorgchem-2017-56-8900.pdf

Maia LB, Moura JJG. "Lessons from denitrification for the human metabolism of signalling nitric oxide." In: Moura I, Moura JJG, Pauleta SR, Maia LB, eds. Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2). Vol. 41. The Royal Society of Chemistry; 2017:. Abstract

The nitric oxide radical ˙NO (NO) is a signalling molecule involved in several physiological processes in humans, including vasodilation, immune response, neurotransmission, platelet aggregation, apoptosis and gene expression. Undue normal conditions, NO synthases catalyse the formation of NO from l-arginine and dioxygen. Yet, upon a hypoxic event, when the decreased dioxygen concentration compromises NO synthase activity, cells can generate NO from another source: nitrite. Since the late 1990s, it has become clear that nitrite can be reduced back to NO under hypoxic/anoxic conditions. Simultaneously, it was realised that nitrite can exert a significant cytoprotective action in vivo during ischaemia and other pathological conditions. Presently, blood and tissue nitrite are recognised as NO “storage forms” that can be made available in order to maintain NO formation and ensure cell signalling and survival under challenging conditions. To reduce nitrite to NO, human cells can use different metalloproteins that are present in cells for carrying out other functions, including several haemic proteins and molybdoenzymes, forming what we refer to as “non-dedicated nitrite reductases”. In this chapter, two non-dedicated nitrite reductases—xanthine oxidase and myoglobin—will be described, and the human nitrate/nitrite/NO signalling pathway will be discussed within the cellular context and the nitrogen cycle scenario.

http://docentes.fct.unl.pt/lblm/files/rsc_book-denitrification-2017-chap_17.pdf

Maia LB, Moura I, Moura JJG. "Molybdenum and tungsten-containing enzymes: an overview." In: Hille R, Schulzke C, Kirk M, eds. Molybdenum and Tungsten Enzymes: Biochemistry, RSC Metallobiology Series No. 5 (ISBN: 978-1-78262-089-1). Vol. 28. The Royal Society of Chemistry; 2017:. Abstract
application/pdf icon_RSC_Book-Mo_W_Enzymes-2017-Chap_1.pdf

Molybdenum is essential to most organisms, being found in the active site of enzymes that catalyze redox reactions involving carbon, nitrogen and sulfur atoms of key metabolites. Some of the molybdenum-dependent reactions constitute key steps in the global biogeochemical cycles of carbon, nitrogen and sulfur, with particular emphasis on the atmospheric dinitrogen fixation into ammonium. Presently, more than 50 molybdoenzymes are known. The great majority are prokaryotic, with eukaryotes holding only a restricted number of molybdoenzymes. Tungsten, probably because of its limited bioavailability, is less used, being found most often in anaerobic thermophilic prokaryotes.

This chapter provides an overview on the molybdo- and tungstoenzymes.
Their physiological context and significance will be described in Section 1.2,where the recent hypothesis that the lack of molybdenum could have been the limiting factor for the life evolution and expansion on early Earth will receive special attention (Section 1.2.1). A brief introduction to the chemical properties that shape the catalytically competent molybdenum/tungsten centres will be made in Section 1.3. In Section 1.4, the enzymes will be grouped in five main families (Sections 1.4.1 to 1.4.5), according to their metal/cofactor structure, and a general view on the structural (section (a)) and mechanistic (section (b)) versatility of each family will be presented. A brief account of novel heteronuclear centres containing molybdenum, whose physiological function is not yet fully understood, will be made in Section 1.4.6. A final outlook on our present knowledge about these enzymes will conclude this chapter.

http://docentes.fct.unl.pt/lblm/files/mo_w_enzymes-rsc_book-chap_1.pdf

Maia LB, Moura I, Moura JJG. "Molybdenum and tungsten-containing formate dehydrogenases: aiming to inspire a catalyst for carbon dioxide utilization." Inorg Chim Acta. 2017;455:350-363. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/ica-2017-455-350.pdf

Maiti BK, Maia L, Pauleta SR, Moura I, Moura JJG. "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." Inorg Chem. 2017;56:2210-2220. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/inorgchem-2017-56-2210.pdf

2016
Maia LB, Moura JJG. "Detection of nitric oxide by electron paramagnetic resonance spectroscopy: spin-trapping with iron-dithiocarbamates." Methods Mol Biol. 2016;1424:81-102. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/methodsmolbiol-2016-1424-81.pdf

Maia LB, Fonseca L, Moura I, Moura JJG. "Reduction of carbon dioxide by a molybdenum-containing formate dehydrogenase: a kinetic and mechanistic study." J Am Chem Soc. 2016;138:8834-8846. Abstract
image/jpeg icon_fdh_mechanism.jpg
Website

http://docentes.fct.unl.pt/lblm/files/jacs-2016-138-8834.pdf

2015
Maiti BK, Maia LB, Silveira CM, Todorovic S, Carreira C, Carepo MS, Grazina R, Moura I, Pauleta SR, Moura JJG. "Incorporation of molybdenum in rubredoxin: models for mononuclear molybdenum enzymes." Journal of Biological Inorganic Chemistry. 2015;20:821-829. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-821.pdf

Moura JJG, Bernhardt PV, Maia LB, Gonzalez PJ. "Molybdenum and tungsten enzymes: from Biology to chemistry and back." Journal of Biological Inorganic Chemistry. 2015;20:181-182. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-181.pdf

Maia LB, Moura JJG, Moura I. "Molybdenum and tungsten-dependent formate dehydrogenases." Journal of Biological Inorganic Chemistry. 2015;20:287-309. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-287.pdf

Maia LB, Pereira V, Mira L, Moura JJG. "Nitrite reductase activity of rat and human xanthine oxidase, xanthine dehydrogenase and aldehyde oxidase: evaluation of their contribution to the NO formation in vivo." Biochemistry. 2015;54:685-710. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/biochemistry-2015-54-685.pdf

Maia LB, Moura JJG. "Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases." Journal of Biological Inorganic Chemistry. 2015;20:403-433. AbstractWebsite

http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-403_1.pdf