Mannich base Cu(II) complexes as biomimetic oxidative catalyst.

Galactose Oxidase (GOase) and catechol oxidase (COase) are the metalloenzymes of copper having monomeric and dimeric sites of coordination, respectively. This paper summarizes the results of our studies on the structural, spectral and catalytic properties of new mononuclear copper (II) complexes [CuL(OAc)] (1), and [CuL] (2), (HL = 2,4‑dichloro‑6‑{[(2'‑dimethyl‑aminoethyl)methylamino]methyl}‑phenol) which can mimic the functionalities of the metalloenzymes GOase and COase. The structure of the compounds has been elucidated by X-ray crystallography and the mimicked Cu(II) catalysts were further characterized by EPR. These mimicked models were used for GOase and COase catalysis. The GOase catalytic results were identified by GC-MS and, analyzed by HPLC at room temperature. The conversion of benzyl alcohol to benzaldehyde were significant in presence of a strong base, BuNOMe in comparison to the neutral medium. Apart from that, despite of being monomeric in nature, both the homogeneous catalysts are very prone to participate in COase mimicking oxidation reaction. Nevertheless, during COase catalysis, complex 1 was found to convert 3,5‑ditertarybutyl catechol (3,5-DTBC) to 3,5‑ditertarybutyl quinone (3,5-DTBQ) having greater rate constant, k or turn over number (TON) value over complex 2. The generation of reactive intermediates during COase catalysis were accounted by electrospray ionization mass spectrometry (ESI-MS). Through mechanistic approach, we found that HO is the byproduct for both the GOase and COase catalysis, thus, confirming the generation of reactive oxygen species during catalysis. Notably, complex 1 having mono-ligand coordinating atmosphere has superior catalytic activity for both cases in comparison to complex 2, that is having di-ligand environment.