Computational analysis of the tryptophan cation radical energetics in peroxidase Compound I.

ABSTRACT: Three well-characterized heme peroxidases (cytochrome c peroxidase = CCP, ascorbate peroxidase = APX, and Leishmania major peroxidase = LMP) all have a Trp residue tucked under the heme stacked against the proximal His heme ligand. The reaction of peroxidases with H₂O₂ to give Compound I results in the oxidation of this Trp to a cationic radical in CCP and LMP but not in APX. Considerable experimental data indicate that the local electrostatic environment controls whether this Trp or the porphyrin is oxidized in Compound I. Attempts have been made to place the differences between these peroxidases on a quantitative basis using computational methods. These efforts have been somewhat limited by the approximations required owing to the computational cost of using fully s

SUBMITTER: Poulos TL 

PROVIDER: S-EPMC8907084 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature