Catalytic galactose oxidase models: biomimetic Cu(II)-phenoxyl-radical reactivity.
Biomimetic functional models of the mononuclear copper enzyme galactose oxidase are presented that catalytically oxidize benzylic and allylic alcohols to aldehydes with O2 under mild conditions. The mechanistic fidelity between the models and the natural system is pronounced. Modest structural mimicry proves sufficient to transfer an unusual ligand-based radical mechanism, previously unprecedented outside the protein matrix, to a simple chemical system.
Wang
Y
Y
Department of Chemistry, Stanford University, Stanford, CA 94305-5080, USA.
DuBois
J L
JL
Hedman
B
B
Hodgson
K O
KO
Stack
T D
TD
D000438:Alcohols / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D003300:Copper / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D005609:Free Radicals; D005692:Galactose Oxidase / Q000737:chemistry* / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism; D008956:Models, Chemical; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D010636:Phenols / Q000737:chemistry / Q000378:metabolism*; D013057:Spectrum Analysis
D000438:Alcohols; D000447:Aldehydes; D005609:Free Radicals; D010636:Phenols; C042329:phenoxy radical; D003300:Copper; D006861:Hydrogen Peroxide; D005692:Galactose Oxidase; D010100:Oxygen