What Drives Radical Halogenation versus Hydroxylation in Mononuclear Nonheme Iron Complexes? A Combined Experimental and Computational Study.

ABSTRACT: Nonheme iron halogenases are unique enzymes in nature that selectively activate an aliphatic C-H bond of a substrate to convert it into C-X (X = Cl/Br, but not F/I). It is proposed that they generate an Fe^III(OH)(X) intermediate in their catalytic cycle. The analogous Fe^III(OH) intermediate in nonheme iron hydroxylases transfers OH^• to give alcohol product, whereas the halogenases transfer X^• to the carbon radical substrate. There remains significant debate regarding what factors control their remarkable selectivity of the halogenases. The reactivity of the complexes Fe^III(BNPA^Ph2O)(OH)(X) (X = Cl, Br) with a secondary carbon radical (R^•) is described. It is found that X^• transfer occurs with a secondar

SUBMITTER: Gerard EF 

PROVIDER: S-EPMC9228086 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature