Crystallographic and spectroscopic characterization of a nonheme Fe(IV)-O complex.
Following the heme paradigm, it is often proposed that dioxygen activation by nonheme monoiron enzymes involves an iron(IV)=oxo intermediate that is responsible for the substrate oxidation step. Such a transient species has now been obtained from a synthetic complex with a nonheme macrocyclic ligand and characterized spectroscopically. Its high-resolution crystal structure reveals an iron-oxygen bond length of 1.646(3) angstroms, demonstrating that a terminal iron(IV)=oxo unit can exist in a nonporphyrin ligand environment and lending credence to proposed mechanisms of nonheme iron catalysis.
Rohde
Jan-Uwe
JU
Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant Street SE, Minneapolis, MN 55455, USA.
In
Jun-Hee
JH
Lim
Mi Hee
MH
Brennessel
William W
WW
Bukowski
Michael R
MR
Stubna
Audria
A
Münck
Eckard
E
Nam
Wonwoo
W
Que
Lawrence
L
D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003460:Crystallization; D018360:Crystallography, X-Ray; D007501:Iron / Q000737:chemistry*; D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization; D015204:Spectroscopy, Mossbauer
D008024:Ligands; C066317:ferryl iron; D007501:Iron; D010100:Oxygen