Intramolecular Charge Transfer and Biomimetic Reaction Kinetics in Galactose Oxidase Model Complexes

• Published in: Journal of the American Chemical Society 2003-07, Vol.125 (29), p.8716-8717
• Main Authors: Pratt, Russell C, Stack, T. Daniel P
• Format: Article
• Language: English
• Subjects: Benzyl Alcohol - chemistry; Biomimetic Materials - chemistry; Biomimetic Materials - metabolism; Chemistry; Copper - chemistry; Copper - metabolism; Exact sciences and technology; Galactose Oxidase - chemistry; Galactose Oxidase - metabolism; Kinetics; Kinetics and mechanisms; Organic chemistry; Organometallic Compounds - chemistry; Organometallic Compounds - metabolism; Oxidation-Reduction; Reactivity and mechanisms; Spectroscopy, Near-Infrared
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/ja035837j

One-electron oxidation of two structurally similar CuII−diphenolate complexes, 1 and 2, creates EPR-silent CuII−phenoxyl complexes [1]+ and [2]+ that mimic the oxidized form of the enzyme galactose oxidase (GOase). Both model complexes display novel NIR absorptions assigned to phenolate−phenoxyl charge transfer that resemble a tyrosinate−tyrosyl charge-transfer band observed in the enzymatic system. [1]+ and [2]+ react with benzyl alcohol to form 0.5 equivs of benzaldehyde per complex; biomimetic reduction to CuI−phenol complexes is not observed, but such species may exist transiently. Initial kinetic studies show that [2]+ reacts faster with benzyl alcohol than does [1]+, despite being a significantly weaker oxidant (ΔE° = 370 mV). This acceleration is ascribed to mechanistic differences:  [2]+ appears to bind substrate prior to the rate-determining step. Large, nonclassical kinetic isotope effects confirm C−H bond cleavage as the rate-determining step in the reactions of both [1]+ and [2]+ with benzyl alcohol, as is the case for GOase.