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M. Costas, M. P. Mehn, M. P. Jensen and L. Que Jr., “Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates,” Chemical Reviews, Vol. 104, No. 2, 2004, pp. 939-986. doi:10.1021/cr020628n

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• TITLE: Recent Advances in X-Ray Structures of Metal-Phenoxyl Radical Complexes

  AUTHORS: Yuichi Shimazaki

  KEYWORDS: Phenoxyl Radical; Metal Complexes; Oxidation; Valence State; Crystal Structure; Electronic Structure; Reactivity

  JOURNAL NAME: Advances in Materials Physics and Chemistry, Vol.3 No.1A, April 26, 2013

  ABSTRACT: An “experimental” valence state of metal complexes is sometime different from the “formal” oxidation state, especially in the species having redox active ligands. This difference can be seen in biological system, such as iron(IV)-porphyrin π-cation radical in some heme proteins and copper(II)-phenoxyl radical in galactose oxidase (GO). Although structural characterizations of these species by X-ray diffraction methods have been rare due to their stability, some artificial metal-phenoxyl radical complexes have been synthesized and successfully characterized by X-ray crystal structure. In this review, syntheses and X-ray crystal structures of the one-electron oxidized metal-phenolate complexes, metal- phenoxyl radical, and high-valent metal phenolate species are discussed.