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    Design, synthesis, characterization, crystal structure, in silico studies, and inhibitory properties of the PEPPSI type Pd(II)NHC complexes bearing chloro/fluorobenzyl group
    (Academic Press Inc Elsevier Science, 2023) Gok, Yetkin; Taslimi, Parham; Sen, Betul; Bal, Selma; Aktas, Aydin; Aygun, Muhittin; Sadeghi, Morteza
    This work contains synthesis, characterization, crystal structure, and biological activity of a new series of the PEPPSI type Pd(II)NHC complexes [(NHC)Pd(II)(3-Cl-py)]. NMR, FTIR, and elemental analysis techniques were used to characterize all (NHC)Pd(II)(3-Cl-py) complexes. Also, molecular and crystal structures of complex 1c were established by single-crystal X-ray diffraction. Regarding the X-ray studies, the palladium(II) atom has a slightly distorted square-planar coordination environment. Additionally, the enzyme inhibitory effect of new (NHC)Pd(II)(3-Cl-py) complexes (1a-1g) was studied. They exhibited highly potent inhibition effect on acetyl -cholinesterase (AChE), butyrylcholinesterase (BChE) and carbonic anhydrases (hCAs) (Ki values are in the range of 0.08 +/- 0.01 to 0.65 +/- 0.06 mu M, 10.43 +/- 0.98 to 22.48 +/- 2.01 mu M, 6.58 +/- 0.30 to 10.88 +/- 1.01 mu M and 6.34 +/- 0.37 to 9.02 +/- 0.72 mu M for AChE, BChE, hCA I, and hCA II, respectively). Based on the molecular docking, among the seven synthesized complexes, 1c, 1b, 1e, and 1a significantly inhibited AChE, BChE, hCA I, and hCA II enzymes, respectively. The findings highpoint that (NHC)Pd(II)(3-Cl-py) complexes can be considered as possible inhibitors via metabolic enzyme inhibition.