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Urease mimetics: catalysis and mechanism comprehension


The use of enzyme mimetics as an alternative to biological catalysts arise due to the possibility of obtaining compounds with higher efficiency and stability (pH, temperature) than an enzyme. Metalloenzymes have their active sites mimicked by the use of coordination compounds as a primary coordination sphere. However, most of the bio-mimetics do not simulate the secondary coordination sphere interactions and consequently, do not exhibit similar catalytic conversions and reaction rates of an enzyme. Urease is a good example of this problem, since despite of the extensive studies of urease bio-mimetics, urea hydrolysis can only be performed in a stequiometric way. This catalytic inability points to the lack of pockets mimicking secondary interactions, which facilitate substrate coordination and hydrolysis. The first report on a complex able to hydrolyze urea catalytically was accomplished by the proponent of this project, who synthesized a binuclear nickel compound with hydrophobic interactions resembling an enzyme active-site. However, although urea hydrolysis is performed by this complex in a similar manner to urease, the reaction rates are much lower and therefore, it is far from optimal. In this project it is proposed to use multifunctional ligands containing phenolate to mimic the primary coordination sphere and modified phenyl groups (-NO2, -COOH,- NH2) or frustrated Lewis pairs (NR3H+/BR3OH-) to mimic the polar secondary coordination sphere of urease. It is expected to obtain efficient mimetics, which would be able to use in C-C coupling reactions. (AU)

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(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
CASTRO, CAIO B.; SILVEIRA, RAFAEL G.; COLOMBARI, FELIPPE M.; DE MOURA, ANDRE FARIAS; NASCIMENTO, OTACIRO R.; MARQUES NETTO, CATERINA G. C.. Solvent Effect on the Regulation of Urea Hydrolysis Reactions by Copper Complexes. CHEMISTRY-SWITZERLAND, v. 2, n. 2, p. 20-pg., . (13/07296-2, 12/15147-4, 16/01622-3)
MODENEZ, IAGO A.; SASTRE, DIEGO E.; MORAES, FERNANDO C.; MARQUES NETTO, CATERINA G. C.. Influence of Glutaraldehyde Cross-Linking Modes on the Recyclability of Immobilized Lipase B from Candida antarctica for Transesterification of Soy Bean Oil. Molecules, v. 23, n. 9, . (16/01622-3, 14/13411-1)

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