Nickel() complexes of a 3N ligand as a model for diketone cleaving unusual nickel()-dioxygenase enzymes

Diketone substrate bound nickel( ii ) complexes of 2,6-bis(1-methylbenzimidazolyl)pyridine have been synthesized and characterized as relevant active site models for unusual diketone cleaving Ni( ii )-dependent enzymes Ni-ARD and DKDO. The average Ni-N py/benzim bond distances (2.050-2.107 Å) of mod...

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Bibliographic Details
Published in:Dalton transactions : an international journal of inorganic chemistry 2018-03, Vol.47 (12), p.449-453
Main Authors: Ramasubramanian, Ramamoorthy, Anandababu, Karunanithi, Kumar, Mukesh, Mayilmurugan, Ramasamy
Format: Article
Language:English
Subjects:
Adducts
Benzoic acid
Coordination compounds
Enzymes
Nickel
Substrates
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Summary:Diketone substrate bound nickel( ii ) complexes of 2,6-bis(1-methylbenzimidazolyl)pyridine have been synthesized and characterized as relevant active site models for unusual diketone cleaving Ni( ii )-dependent enzymes Ni-ARD and DKDO. The average Ni-N py/benzim bond distances (2.050-2.107 Å) of model complexes are almost identical to the Ni-N His bond distances of Ni II -ARD (2.02-2.19 Å). The reaction of these adducts with dioxygen exhibited C-C cleavage with the rate of k O 2 , 5.24-73.71 × 10 −3 M −1 s −1 . The phenyl substituted adduct regioselectively elicits 52% of benzoic acid as the major product. The substrate-bound nickel( ii ) complexes of the 3N ligand are synthesized as the models for Ni( ii )-dependent enzymes. They exhibited regioselective C-C cleavage using dioxygen.
ISSN:1477-9226
1477-9234
DOI:10.1039/c7dt04739h