Computational study for the biomimetic reactivity of the structural analogue for the resting state of the active site of the nickel acireductone dioxygenase (Ni-ARD) is presented. A series of complexes with the n4o motif mimics the contribution of the glutamate and histidine enzymatic residue. Various substrate including acireductone and related compounds are used to assess the enzyme substrate interaction with dioxygen. Computational calculations are performed using BP86 functional and 631+G(d) basis set. IRC calculations were used to confirm that transition states lead to desired intermediate. We have proposed a mechanism for oxygen insertion and C-C bond cleavage and results are presented here.

Computational study for understanding the action of nickle acireductone dioxygenase (Ni-ARD) through a biomimietic structural modeling

2019 Spring National Meeting

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