The first structural models of the proposed -Fe(OH)(halide) intermediate in the non-heme iron halogenases were synthesized and examined for their inherent reactivity with tertiary carbon radicals. Selective hydroxylation occurs for these -Fe(OH)(X) (X = Cl, Br) complexes in a radical rebound-like process. In contrast, a -Fe(Cl) complex reacts with carbon radicals to give halogenation. These results are discussed in terms of the inherent reactivity of the analogous rebound intermediate in both enzymes and related catalysts.