L
Lígia O. Martins
Researcher at Universidade Nova de Lisboa
Publications - 99
Citations - 4768
Lígia O. Martins is an academic researcher from Universidade Nova de Lisboa. The author has contributed to research in topics: Laccase & Bacillus subtilis. The author has an hindex of 35, co-authored 90 publications receiving 4242 citations. Previous affiliations of Lígia O. Martins include Universidade Lusófona & University of Coimbra.
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Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology
TL;DR: This review aims to present an update of current knowledge on prokaryotic multicopper oxidases, with a special emphasis on laccases, anticipating their enormous potential for industrial and environmental applications.
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Mechanisms underlying dioxygen reduction in laccases. Structural and modelling studies focusing on proton transfer
Isabel Bento,Catarina Silva,Zhenjia Chen,Lígia O. Martins,Peter F. Lindley,Cláudio M. Soares +5 more
TL;DR: Evidence is presented that Glu 498 is the only proton-active group in the vicinity of the trinuclear centre, which strongly suggests that this residue may be responsible for channelling the protons needed for the reduction of dioxygen to water.
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Proximal mutations at the type 1 copper site of CotA laccase: spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants
Paulo Durão,Zhenjia Chen,Catarina Silva,Cláudio M. Soares,Manuela M. Pereira,Smilja Todorovic,Peter Hildebrandt,Isabel Bento,Peter F. Lindley,Lígia O. Martins +9 more
TL;DR: Overall the data clearly indicate that the Ile(494) mutation causes a major alteration of the structure near the type 1 copper site and this has been confirmed by X-ray crystallography.
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Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase.
Lígia O. Martins,Nuno Empadinhas,Joey D. Marugg,Carla Miguel,Célia Ferreira,Milton S. da Costa,Helena Santos +6 more
TL;DR: The mannosylglycerate synthase enzyme was purified and characterized, and the corresponding mgs gene was identified from a genomic library of R. marinusis with high yield and had a molecular mass of 46,125 Da, and was specific for GDP mannose andd-glycerates.
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Synergistic action of azoreductase and laccase leads to maximal decolourization and detoxification of model dye-containing wastewaters.
Sónia Mendes,Ana Paula Farinha,Christian G. Ramos,Jorge H. Leitão,Jorge H. Leitão,Cristina A. Viegas,Cristina A. Viegas,Lígia O. Martins +7 more
TL;DR: The azoreductase PpAzoR from Pseudomonas putida shows a broader specificity for decolourization of azo dyes than CotA-laccase from Bacillus subtilis, and is a promising candidate for the biological treatment of industrial dye containing effluents.