Axial ligand tuning of a nonheme iron(IV)-oxo unit for hydrogen atom abstraction.
The reactivities of mononuclear nonheme iron(IV)-oxo complexes bearing different axial ligands, [Fe(IV)(O)(TMC)(X)](n+) [where TMC is 1,4,8,11-tetramethyl-1,4,8,11-tetraazacyclotetradecane and X is NCCH(3) (1-NCCH(3)), CF(3)COO(-) (1-OOCCF(3)), or N(3)(-) (1-N(3))], and [Fe(IV)(O)(TMCS)](+) (1'-SR) (where TMCS is 1-mercaptoethyl-4,8,11-trimethyl-1,4,8,11-tetraazacyclotetradecane), have been investigated with respect to oxo-transfer to PPh(3) and hydrogen atom abstraction from phenol O H and alkylaromatic C H bonds. These reactivities were significantly affected by the identity of the axial ligands, but the reactivity trends differed markedly. In the oxidation of PPh(3), the reactivity order of 1-NCCH(3) > 1-OOCCF(3) > 1-N(3) > 1'-SR was observed, reflecting a decrease in the electrophilicity of iron(IV)-oxo unit upon replacement of CH(3)CN with an anionic axial ligand. Surprisingly, the reactivity order was inverted in the oxidation of alkylaromatic C H and phenol O H bonds, i.e., 1'-SR > 1-N(3) > 1-OOCCF(3) > 1-NCCH(3). Furthermore, a good correlation was observed between the reactivities of iron(IV)-oxo species in H atom abstraction reactions and their reduction potentials, E(p,c), with the most reactive 1'-SR complex exhibiting the lowest potential. In other words, the more electron-donating the axial ligand is, the more reactive the iron(IV)-oxo species becomes in H atom abstraction. Quantum mechanical calculations show that a two-state reactivity model applies to this series of complexes, in which a triplet ground state and a nearby quintet excited-state both contribute to the reactivity of the complexes. The inverted reactivity order in H atom abstraction can be rationalized by a decreased triplet-quintet gap with the more electron-donating axial ligand, which increases the contribution of the much more reactive quintet state and enhances the overall reactivity.
Sastri
Chivukula V
CV
Department of Chemistry, Division of Nano Sciences, and Center for Biomimetic Systems, Ewha Womans University, Seoul 120-750, Korea.
Lee
Jimin
J
Oh
Kyungeun
K
Lee
Yoon Jin
YJ
Lee
Junghyun
J
Jackson
Timothy A
TA
Ray
Kallol
K
Hirao
Hajime
H
Shin
Woonsup
W
Halfen
Jason A
JA
Kim
Jinheung
J
Que
Lawrence
L
Shaik
Sason
S
Nam
Wonwoo
W
D006859:Hydrogen / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D008024:Ligands; D019159:Nonheme Iron Proteins / Q000737:chemistry*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry*
C505853:(FeIV(O)(TMCS))+; D008024:Ligands; D019159:Nonheme Iron Proteins; D013438:Sulfhydryl Compounds; C066317:ferryl iron; D006859:Hydrogen; D007501:Iron; D010100:Oxygen