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- Title
A Small-molecule Model System of Galactose Oxidase: Geometry, Reactivity, and Electronic Structure.
- Authors
Wendt, Franziska; Rolff, Malte; Thimm, Wulf; Näther, Christian; Tuczek, Felix
- Abstract
The active site of galactose oxidase (GOase) contains a copper atom coordinated by a tyrosyl radical. This enzyme catalyzes the two-electron oxidation of alcohols to aldehydes. We present a GOase model system, which catalytically mediates the conversion of ethanol to acetaldehyde with a TON of 74. The crystal structure of the mononuclear copper complex [CuII( L6- H)(CH3CN)](ClO4)2 coordinated by acetonitrile reveals an apical position for the phenol group. Furthermore we prepared the dimeric complex [(CuII)2( L6)2](PF6)2, which was structurally characterized as well. Cleavage of the dimer along with formation of the phenoxyl radical was effected by cerium(IV) ammonium nitrate. The dimer could also be cleaved by treatment with pyridine. In order to obtain information about the interaction between the unpaired electron in the d-orbital of CuII to the electron in the half-occupied orbital of the tyrosyl radical DFT is employed. In the ground state a ferromagnetic coupling ( S = 1) is obtained.
- Subjects
GALACTOSE oxidase; ELECTRONIC structure; DIMERIC ions; ACETALDEHYDE derivatives; CRYSTAL structure; MOLECULAR structure of acetonitrile; COPPER compounds; CRYSTALLOGRAPHY
- Publication
Zeitschrift für Anorganische und Allgemeine Chemie, 2013, Vol 639, Issue 14, p2502
- ISSN
0044-2313
- Publication type
Article
- DOI
10.1002/zaac.201300475