A glass was made using bottom ash produced by a Portuguese municipal solid waste (MSW) incinerator. The bottom ash was the single batch material used in the formation of the glass, which was obtained through a conventional melt-quenching method. The glass was then converted to glass-ceramic for further recycling to construction materials. After submitting the glass samples to several heat treatments, between 820 and 1050°C and during different times, it was verified that the optimum heat treatment schedule for the ceramization of the glass was at 1000°C for 10h, as confirmed by microstructural observation and by X-ray diffraction. The major crystalline phases precipitated in the glass-ceramic were wollastonite (CaSiO3) and diopside (Ca(Mg,Al)(Si,Al)2O6). Microstructural analysis of the glass-ceramic revealed that the crystalline phases were present as dendrites and fiber-like structures that were homogeneously distributed in the material. The glassceramic showed good mechanical properties with a hardness of 5.6 MPa and a bending strength of 101 MPa. This material had a density of 2.8 gcm-3 and a thermal expansion coefficient of 9.10-6°C-1. The glass and the glass-ceramic showed an excellent chemical stability against leaching in acidic solution and in alkaline solution. In summary, both the glass and the glass-ceramic have good chemical and mechanical properties and can, therefore, be applied as construction materials.

The gene for pseudoazurin was isolated from Paracoccus pantotrophus LMD 52.44 and expressed in a heterologous system with a yield of 54.3 mg of pure protein per liter of culture. The gene and protein were shown to be identical to those from P. pantotrophus LMD 82.5. The extinction coefficient of the protein was re-evaluated and was found to be 3.00 mM(-1) cm(-1) at 590 nm. It was confirmed that the oxidized protein is in a weak monomer/dimer equilibrium that is ionic- strength-dependent. The pseudoazurin was shown to be a highly active electron donor to cytochrome c peroxidase, and activity showed an ionic strength dependence consistent with an electrostatic interaction. The pseudoazurin has a very large dipole moment, the vector of which is positioned at the putative electron-transfer site, His81, and is conserved in this position across a wide range of blue copper proteins. Binding of the peroxidase to pseudoazurin causes perturbation of a set of NMR resonances associated with residues on the His81 face, including a ring of lysine residues. These lysines are associated with acidic residues just back from the rim, the resonances of which are also affected by binding to the peroxidase. We propose that these acidic residues moderate the electrostatic influence of the lysines and so ensure that specific charge interactions do not form across the interface with the peroxidase.