Fe(III)-Complex-Imprinted Polymers for the Green Oxidative Degradation of the Methyl Orange Dye Pollutant.

One of the biggest problems worldwide is the pollution of natural water bodies by dyes coming from effluents used in the textile industry. In the quest for novel effluent treatment alternatives, the aim of this work was to immobilize Fe(III) complexes in molecularly imprinted polymers (MIPs) to produce efficient Fenton-like heterogeneous catalysts for the green oxidative degradation of the methyl orange (MO) dye pollutant. Different metal complexes bearing commercial and low-cost ligands were assayed and their catalytic activity levels towards the discoloration of MO by H2O2 were assessed. The best candidates were Fe(III)-BMPA (BMPA = di-(2-picolyl)amine) and Fe(III)-NTP (NTP = 3,3',3″-nitrilotripropionic acid), displaying above 70% MO degradation in 3 h. Fe(III)-BMPA caused the oxidative degradation through two first-order stages, related to the formation of BMPA-Fe-OOH and the generation of reactive oxygen species. Only the first of these stages was detected for Fe(III)-NTP. Both complexes were then employed to imprint catalytic cavities into MIPs. The polymers showed catalytic profiles that were highly dependent on the crosslinking agent employed, with N,N-methylenebisacrylamide (MBAA) being the crosslinker that rendered polymers with optimal oxidative performance (>95% conversion). The obtained ion-imprinted polymers constitute cheap and robust solid matrices, with the potential to be coupled to dye-containing effluent treatment systems with synchronous H2O2 injection.

CYP154C5 Regioselectivity in Steroid Hydroxylation Explored by Substrate Modifications and Protein Engineering*.

CYP154C5 from Nocardia farcinica is a P450 monooxygenase able to hydroxylate a range of steroids with high regio- and stereoselectivity at the 16α-position. Using protein engineering and substrate modifications based on the crystal structure of CYP154C5, an altered regioselectivity of the enzyme in steroid hydroxylation had been achieved. Thus, conversion of progesterone by mutant CYP154C5 F92A resulted in formation of the corresponding 21-hydroxylated product 11-deoxycorticosterone in addition to 16α-hydroxylation. Using MD simulation, this altered regioselectivity appeared to result from an alternative binding mode of the steroid in the active site of mutant F92A. MD simulation further suggested that the entrance of water to the active site caused higher uncoupling in this mutant. Moreover, exclusive 15α-hydroxylation was observed for wild-type CYP154C5 in the conversion of 5α-androstan-3-one, lacking an oxy-functional group at C17. Overall, our data give valuable insight into the structure-function relationship of this cytochrome P450 monooxygenase for steroid hydroxylation.