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Ten Years of a Biomimetic Approach to the Copper(II) Radical Site of Galactose Oxidase (Eur. J. Inorg. Chem. 17/2007)
Author(s) -
Thomas Fabrice
Publication year - 2007
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.200790031
Subject(s) - chemistry , galactose oxidase , bioinorganic chemistry , radical , active site , copper , copper protein , stereochemistry , photochemistry , galactose , enzyme , organic chemistry
The cover picture shows shows the active site of Galactose Oxidase, as it was crystallized in the middle of the 1990s. Its active form featured an unprecedented copper(II)‐tyrosyl (Tyr272 · ) radical system. Since 1996, several model compounds of this entity have been developed worldwide. They contributed significantly to the enhanced understanding of the spectral properties, structural attributes, and even to the reactivity of the enzyme's active site. Four prototypical complexes are shown; each of them is representative of the main classes of ligands developed (tripodal, salen, TACN, and iminosemiquinone scaffolds). Phenoxyl radicals typically exhibit absorption bands at around 420 and 600−800 nm, as shown in the UV/Vis spectrum. Ten years of this bioinorganic story is discussed in the Microreview by F. Thomas on p. 2379 ff.