Two iron phenolate complexes have been synthesized to serve as models for dioxygenase enzyme-substrate and enzyme-inhibitor interactions; their X-ray structures have been determined. Fe(saloph)catH, a monodentate catecholate complex, crystallizes in the triclinic space group P1̄ (a = 9.960 (6) Å, b = 8.108 (3) Å, c = 13.849 (8) Å, α = 95.73 (4)°, β = 91.93 (5)°, γ = 72.13 (4)°), while [Fe(salen)]2hq, a bridged hydroquinone complex, crystallizes in the orthorhombic space group Pbca (a = 12.917 (3) Å, b 13.100 (4) Å, c = 19.440 (4) Å, α = β = γ = 90°). The irons in both complexes exhibit properties typical of square-pyramidal geometry—metal atom raised above the basal mean plane (0.55 Å for Fe(saloph)catH and 0.50 Å for [Fe(salen)]2hq) and short apical Fe-O bonds (1.828 (4) Å for Fe(saloph)catH and 1.861 (2) Å for [Fe(salen)]2hq). The average Fe-O and Fe-N bond lengths in the two tetradentate ligands are the same in both structures (1.905 and 2.079 Å, respectively) and are in excellent agreement with those found for similar complexes. Fe(saloph)catH and [Fe(salen)]2hq represent the first monodentate catecholate and the first bridged hydroquinone structures, respectively, of iron(III).