Local Electric Fields as a Natural Switch of Heme-Iron Protein Reactivity.

ABSTRACT: Heme-iron oxidoreductases operating through the high-valent Fe^IVO intermediates perform crucial and complicated transformations, such as oxidations of unreactive saturated hydrocarbons. These enzymes share the same Fe coordination, only differing by the axial ligation, e.g., Cys in P450 oxygenases, Tyr in catalases, and His in peroxidases. By examining ~200 heme-iron proteins, we show that the protein hosts exert highly specific intramolecular electric fields on the active sites, and there is a strong correlation between the direction and magnitude of this field and the protein function. In all heme proteins, the field is preferentially aligned with the Fe-O bond ( F_z ). The Cys-ligated P450 oxygenases have the highest average F_z </

SUBMITTER: Bim D 

PROVIDER: S-EPMC8372207 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature