Luisa Maia

PhD Researcher, FCT NOVA
Email: luisa.maia(at)fct.unl.pt
Tel: + 351 21 294 83 00, ext. 10927
Webpage: Luisa's webpage

Research Activities - Keywords
< more info can be found at Luisa's webpage >
• Metalloenzymes, structure-activity relationships
• Reactive oxygen and nitrogen species (ROS/RNS) biochemistry
    - formation/elimination and enzymes structure-activity relationships
• Mechanisms of ROS/RNS-mediated diseases
• New catalytic activities of molybdoenzymes
    - NADH oxidation, nitrite reduction, nitric oxide formation, carbon dioxide reduction (carbon dioxide scavenging)
    - structural and mechanistic studies (mammalian and bacterial enzymes)
    - in situ studies (mammalian enzymes)
• Xanthine oxidase, xanthine dehydrogenase, aldehyde oxidase, aldehyde oxidoreductase,
    superoxide dismutase, catalase
    mammalian (rat, bovine and human liver, blood and milk) and bacterial sources (Desulfovibrio bacteria)

Teaching Interests
• Biochemistry, Bioinorganic, Biophysics, Enzymology
• EPR Spectroscopy (applications to Chemistry, Biology and Medicine)
• Undergraduate, Master and PhD programs
• Science divulgation

Selected References
< a full list can be found at RID F-8106-2011 or at Scopus >

• Lessons from denitrification for the human metabolism of signalling nitric oxide
Maia LB, Moura JJG
in Metalloenzymes in Denitrification: Applications and Environmental Impacts,
Eds Moura, I, Moura JJG, Pauleta SR, Maia L,
RSC Metallobiology Series No. 9. (2017) (ISBN: 978-1-78262-376-2),
The Royal Society of Chemistry (DOI: 10.1039/9781782623762-00419)

• Molybdenum and tungsten-containing formate dehydrogenases: aiming to inspire a catalyst for carbon dioxide utilization
Maia LB, Moura I, Moura JJG
Inorg Chim Acta (2017) 455: 350-363 (DOI: 10.1016/j.ica.2016.07.010)

• Reduction of carbon dioxide by a molybdenum-containing formate dehydrogenase: a kinetic and mechanistic study
Maia LB, Fonseca L. Moura I, Moura JJG
JACS (2016) 138: 8834-8846 (DOI: 10.1021/jacs.6b03941)

• Nitrite reductase activity of rat and human xanthine oxidase, xanthine dehydrogenase, and aldehyde oxidase: evaluation of their contribution to NO formation in vivo
Maia LB, Pereira V, Mira L, Moura JJG
Biochemistry (2015) 54: 685-710 (DOI: 10.1021/bi500987w)

• Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases
Maia LB, Moura JJG
J Biol Inorg Chem (2015) 20: 403-433 (DOI: 10.1007/s00775-014-1234-2)
(Link to enhanced PDF: http://rdcu.be/mEXy)

• How Biology handles nitrite
Maia LB, Moura JJG
Chem Rev (2014) 114: 5273-5357 (DOI: 10.1021/cr400518y)

Back to People