Abstract
AbstractCatecholase activity of dicopper(II) complexes containing different numbers of chelate members in the pyridine groups of the ligand was studied to identify a functional model for copper enzyme catechol oxidase. Complexes [CuII(μ‐OH)CuII(L1)](ClO4) (1), [CuII(μ‐OH)CuII(L2)](ClO4) (2), and [CuII(μ‐OH)CuII(L3)](ClO4) (3) were synthesized and characterized by elemental analysis, FTIR, UV–Vis spectroscopy, mass spectrometry, and electrochemistry. Their catalytic activity in the oxidation of 3,5‐di‐tert‐butylcatechol was determined. Changing the number of members of the chelate rings altered the catalytic activity. Complex 2 showed the highest catalytic activity due to a high turnover rate, with efficiency of 3.40±0.61. Mechanistic investigations indicate that the catalytic reaction occurs through the reduction of Cu(II) to Cu(I) with formation of hydrogen peroxide. The spectroscopic and catecholase activity were further rationalized through DFT and TD‐DFT calculations. Interestingly, all three complexes also showed DNA binding properties, which were also corroborated via molecular docking studies.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
