Oxidative dehalogenation of trichlorophenol catalyzed by a promiscuous artificial heme-enzyme
Gerardo Zambrano, Alina Sekretareva, Daniele D’Alonzo, Linda Leone, Vincenzo Pavone, Angela Lombardi, Flavia Nastri
Abstract
], similarly to peroxidase compound I (Cpd I). Addition of TCP to Cpd I rapidly leads to the formation of the corresponding quinone, while Cpd I decays back to the ferric resting state in the absence of substrate. EPR data suggest a catalytic mechanism involving two consecutive one-electron reactions. All results highlight the value of the miniaturization strategy for the development of chemically stable, highly efficient artificial metalloenzymes as powerful catalysts for the oxidative degradation of toxic pollutants.
Topics & Concepts
HalogenationHemeOxidative phosphorylationChemistryEnzymeCombinatorial chemistryArtificial enzymeOxidative enzymeBiochemistryOrganic chemistryEnvironmental remediation with nanomaterialsMetal-Catalyzed Oxygenation MechanismsMicrobial bioremediation and biosurfactants