Abstract

Cu(amino acid) complexes were immobilised on silica gel by covalent anchoring. The amino acids were l-histidine and l-tyrosine and their BOC—( tert-butoxycarbonyl) or methyl ester protected derivatives. To gain control over the synthesis the appropriately protected amino acid was reacted with chloropropylated silica gel first. This modified material as is, or after deprotecting the anchored amino acids, was used in further steps of building the immobilised Cu(II) complex. The covalently grafted complexes were studied by FT-IR spectroscopy and computer modelling. Materials containing protected histidine ligands showed catalase activity (decomposition of H 2O 2), those containing protected or unprotected tyrosine ligands displayed tyrosinase activity (the decomposed H 2O 2 oxidised the tyrosine skeleton to a quinoidal structure).

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call