Oxidative dehalogenation of trichlorophenol catalyzed by a promiscuous artificial heme-enzyme.

ABSTRACT: The miniaturized metalloenzyme Fe(iii)-mimochrome VI*a (Fe(iii)-MC6*a) acts as an excellent biocatalyst in the H₂O₂-mediated oxidative dehalogenation of the well-known pesticide and biocide 2,4,6-trichlorophenol (TCP). The artificial enzyme can oxidize TCP with a catalytic efficiency (k _cat/K ^TCP _m = 150 000 mM^-1 s^-1) up to 1500-fold higher than the most active natural metalloenzyme horseradish peroxidase (HRP). UV-visible and EPR spectroscopies were used to provide indications of the catalytic mechanism. One equivalent of H₂O₂ fully converts Fe(iii)-MC6*a into the oxoferryl-porphyrin radical cation intermediate [(Fe(iv)[double bond, length as m-dash]O)por˙⁺], similar

SUBMITTER: Zambrano G 

PROVIDER: S-EPMC9067433 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature