Catarina S. Silva

Proximal mutations at the type 1 copper site of CotA laccase: spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants.

Manuela M. Pereira, C. Soares, P. Hildebrandt, 2008, The Biochemical journal.

Endo-β-D-1,4-mannanase from Chrysonilia sitophila displays a novel loop arrangement for substrate selectivity.

Ricardo Coelho, Daniele de Sanctis, D. de Sanctis, 2012, Acta crystallographica. Section D, Biological crystallography.

STRUCTURE-FUNCTION ANALYSIS OF MULTI-COPPER OXIDASES

Catarina S. Silva, 2013 .

Crystal structure of the multicopper oxidase from the pathogenic bacterium Campylobacter jejuni CGUG11284: characterization of a metallo-oxidase.

A. Fillat, P. Durão, L. O. Martins, 2012, Metallomics : integrated biometal science.

Mechanisms underlying dioxygen reduction in laccases. Structural and modelling studies focusing on proton transfer

C. Soares, L. O. Martins, P. Lindley, 2010, BMC Structural Biology.

The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis.

Manuela M. Pereira, P. Hildebrandt, P. Durão, 2010, Dalton transactions.

The role of Asp116 in the reductive cleavage of dioxygen to water in CotA laccase: assistance during the proton-transfer mechanism.

C. Soares, J. Damas, L. O. Martins, 2012, Acta crystallographica. Section D, Biological crystallography.

The removal of a disulfide bridge in CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability

Manuela M. Pereira, L. O. Martins, P. Lindley, 2011, JBIC Journal of Biological Inorganic Chemistry.

Endo-β-D-1,4-mannanase from Chrysonilia sitophila displays a novel loop arrangement for substrate selectivity.

D. de Sanctis, I. Bento, R. Coelho, 2012, Acta crystallographica. Section D, Biological crystallography.