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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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Journal ArticleDOI

Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat.

Lígia O. Martins, +7 more
- 24 May 2002 - 
TL;DR: This model of CotA contains all the structural features of a laccase, including the reactive surface-exposed copper center (T1) and two buried copper centers (T2 and T3), and shows a half-life of inactivation at 80 °C of about 4 and 2 h, indicating that CotA is intrinsically highly thermostable.
Journal ArticleDOI

Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties.

Francisco J. Enguita, +4 more
- 23 May 2003 - 
TL;DR: Comparisons with the structure of other monomeric multicopper oxidases containing four copper atoms suggest that CotA may accept the largest substrates of any known laccase, and unlike other laccases, CotA appears to have a flexible lidlike region close to the substrate-binding site that may mediate substrate accessibility.
Journal ArticleDOI

Copper incorporation into recombinant CotA laccase from Bacillus subtilis: characterization of fully copper loaded enzymes.

Paulo Durão, +9 more
- 01 Feb 2008 - 
TL;DR: EPR and resonance Raman data indicate that, presumably, folding in the presence of copper is indispensable for the correct structure of the trinuclear copper-containing site.
Journal ArticleDOI

Organic solutes in hyperthermophilic archaea.

Lígia O. Martins, +5 more
- 01 Mar 1997 - 
TL;DR: The accumulation of organic solutes under optimum growth conditions in 12 species of thermophilic and hyperthermophilic Archaea belonging to the Crenarchaeota and Eury Archaeota was examined, and prominent among them was a compound identified as di-glycerol-phosphate.
Journal ArticleDOI

Perturbations of the T1 copper site in the CotA laccase from Bacillus subtilis: structural, biochemical, enzymatic and stability studies.

Paulo Durão, +5 more
- 21 Apr 2006 - 
TL;DR: X-ray structural comparison of M502L and M502F mutants with the wild-type CotA shows that the geometry of the T1 copper site is maintained as well as the overall fold of the proteins, indicating a key role in the regulation of CotA laccase activity.